STATIC BIOCHEMISTRY
ChapterIV.2.
Proteins are polymers that do not decompose, the minimum structural unit of them is an amino acid (AA). Amino acids are bound together by a peptide linkage. In nature, it grows richer than AK, lower to enter the warehouse of creatures and growing whites. So, non-protein AAs can be eliminated in peptide antibiotics or in intermediate products of protein metabolism. Before the stock of proteins, 20 AAs are included in the alpha form, mixed with different ones, but clearly indicated for the skin protein of the sequence.
1) Aliphatic - glycine (Gli), alanine (Ala), valine (Val), leucine (Leu), isoleucine (Iley);
2) Hydroxy acids - serine (Ser), threanine (Tre);
3) Dicarboxylic - asparagine (Asp), glutamine (Glu), aspartic acid (Ask), glutamic acid (Gla);
4) Bibasic - lysine (Liz), histidine (His), arginine (Arg);
5) Aromatic - phenylalanine (Phen), tyrosine (Tyr), tryptophan (Three);
6) Serkovmіsnі - cysteine (Cis), methionine (Met).
From the biochemical role:
1) glucogenous - through low chemical transformations, go to the pathways of glycolosis (glucose oxidation) - Gli, Ala, Tre, Val, Ask, Glk, Arg, Gis, Met.
2) ketogenic - take part in the enlightenment of ketone bodies - Lei, Iley, Tyr, Fen.
For replacement:
1) Nezaminnі - not synthesized in organisms - Hys, Ili, Leu, Liz, Met, Fen, Tre, Tri, Val, and in young animals Arg, Hys.
2) Replacements - іnshі.
In terms of the visibility of the AA molecule, it is simultaneously amino and carboxyl groups with semiacidic acid-base power. In the neutral middle, AK is found in apparently bipolar ions. color-ioniv tobto.
Not NH 2 - R - COOH, and NH 3 + - R - COO -
Illumination of the peptide bond . As the carboxyl group of one AA acylues the amino group other than AA, as the amide linkage is established, it is called a peptide. That. peptidides are half-shells, created from excess alpha-AA, linked together peptide bond.
Tsej vyazok dosit stabіlniy i razryv yogo vіdbuvaєtsya only for the participation of catalysts - specific enzymes. For the help of such a link, AK are united in dosing long lances, as they are called polypeptides. The skin of such a lance can be revenged on one end of the AK from the free amino group - tse N -terminal surplus, and on the other hand with a carboxyl group - C-terminal surplus.
Polypeptides, which spontaneously form and enhance a single expanse structure, as they are called conformations, are brought to proteins. Stabilization of such a structure is only possible if the polypeptides reach the age of the song, so the polypeptides with a molecular weight of more than 5,000 Da are called proteins. (1 So dear 1/12 to the carbon isotope). Tilki, looming the song of the expanse of life, the white can function.
1) Structural (plastic) - with proteins made up of rich cellular components, and in complexes with lipids, stench enters the warehouse of cellular membranes.
2) Catalytic - all biological catalysts - enzymes for their chemical nature - proteins.
3) Transport - the hemoglobin protein transports oxygen, a number of other proteins that support the complex with lipids transport them through the blood and lymph (butt: myoglobin, syrovatkovy albumin).
4) Mechanochemical - m'yazova robot and іnshі forms ruhu on organisms zdіysnyuyutsya with the participation of fast-moving proteins with vikoristannya macroenergic links (butt: actin, myosin).
5) Regulatory - a number of hormones and other biologically active speeches have a protein nature (insulin, ACTH).
6) Zahisna - antibodies (immunoglobulins) with proteins, moreover, collagen protein becomes the basis of skin, and creatine - hair. The skin that hairs protect the inner core of the body from the outer effusions. Mucoproteins enter the mucosal folds and synovial rіdini.
7) The support is a tendon, the surface of the loams on the sides of the cysts is made up of a significant world of protein speeches (eg: collagen, elastin).
8) Energetic - amino acids of the protein can be found on the way to glycol, which provides energy for the cell.
9) Receptor - rich proteins take part in the processes of vibratory recognition (receptors).
equal organization of the protein molecule.
In the current literature, it is customary to consider 4 equal organization of the structure of the protein molecule.
The sequence of amino acid residues, which are joined together by a peptide link, is called first line organization of the protein molecule. It is encoded by the structural gene of the skin protein. Stars: peptide and disulfide patches between closely packed cysteine surpluses. These covalent interactions, which are less likely to be destroyed by the action of proteolytic enzymes (pepsin, trypsin, too).
The secondary structure is called the expanse of separation of atoms in the head lance of the protein molecule . There are three types of secondary structure: alpha-helix, beta-folding and beta-vigin. It settles down at the expanse for the rahunok of the establishment of water connections between the AK main lancer groupings. Water bonds are formed between the electronegative atoms of acidic carbonyl groups and water atoms of two amino acids.
Alpha spiral– chain-peptide lancet with corkscrew-like twists around a conspicuous cylinder. The diameter of such a spiral is 0.5 A. In natural proteins, a spiral is revealed more than right. Deyakі proteins (insulin) mayut two parallel coils. Beta warehouse– polypeptide lancet folds at the equal fold. Beta-vigin - is mixed with triple amino acids for a watery connection. Vіn necessery change in the space expansion of the polypeptide lanceolate with the established tertiary structure of the protein.
Tretinna structure - the goal of the power of this protein is the way of laying the lanceug polypeptide in the open space . This is the basis of the functionality of the protein. It will ensure the stability of the great protein dealers, which are formed from the impersonal amino acid reserves of those protein groups. Such ordering in the expanse of the cell of the protein is formed by the active centers of the enzymes and the binding of the tertiary structure to the loss of the functional activity of the protein.
The stability of the tertiary structure is more important than non-covalent interactions in the middle of the protein globule - more important than water bonds and van der Waals forces. Ale deyakі proteins dodatkovo stabilizuyutsya for rahunok such covalent vzaєmodіy like disulfide mіstki between surpluses of cysteine.
The greater number of protein molecules can act like alpha helices, as well as beta folding frequencies. And most of all, the globular proteins are formed by the form of the tertiary structure - it is more important that alpha-helices are formed and the shape of the ellipse (more enzymes) is formed. І fibrillary - which are formed more importantly from beta-folding frequency and may be flattened or thread-like form (pepsin, proteins of good cartilage).
Placement in the expanse of mutually interacting sub-units, established with the help of polypeptide lancets, is called quarter structure . Tobto. in the molded quarter structure, it is not the peptide lances that take the part of the power forces, but the globules, which are saturated with the skin s cich kil okremo. The quaternary structure is the main line of organization of the protein molecule and veins attached to far from all proteins. The bonds that form this structure are non-covalent: water, electrostatic interplay.
The fundamental principle of molecular biology: the sequence of amino acid residues of the polypeptide lance of the protein to take all the information in itself, as is necessary for the formation of a simple space structure. Tobto. amino acid sequence, which is in this protein, signifies the adoption of alpha- or beta-conformation of the secondary structure for the settlement between AA water and disulfide bonds and in the distant formation of globular or fibrillary ї structures are also for the structure of non-covalent interactions between biological sites of appointments.
The expansion of the protein is brought to the expansion of the IUD and draws a number of dominance of hydrophilic columns: high diffusion, high viscosity, dangerousness, give Tyndall's cone.
1) Amphotericityis associated with presence in the protein molecule of cationic groups - amino group and anionic - carboxyl groups. The sign of the charge of a molecule to lie in a number of large groups. If the carboxyl groups are more important, then the charge of the molecule is negative (the power of a weak acid is manifested), if the amino group is positive (the main power).
The charge of the protein is deposited in the pH of the medium. In the acidic medium, the molecule acquires a positive charge, in the puddle - negative.
[NH3 + -R-COO - ] 0
pH > 7 [OH - ]7>pH [ H + ]
[ NH 2 - R - COO -] - [NH 3 + - R - COOH] +
The pH value at which the number of different charges in the protein molecules is the same, so the total charge is equal to zero. isoelectric point what protein. The stability of a protein molecule to the influx of physical and chemical factors at the isoelectric point is the least.
The greater number of natural proteins is due to the significant quantity of dicarboxylic amino acids and to this, to lie down to sour proteins. This isoelectric point lies near the slightly acidic medium.
2) rozchini bіlkіv mayut buffer with them authorities for the account of their amphotericity.
3) rozchinnist. If the protein molecule contains polar amino - and carboxyl groups, then in various surface excesses of AA are hydrated - the solution is coacervate.
4) coacervation- exasperation of the water shells of a few particles, without destroying the particles themselves.
5) coagulation- Gluing white particles and falling them into a siege. Tse vіdbuvaєtsya at vydalnі їх іх dratnoї shell. For which it is enough to change the structure of a part of the protein, so that the hydrophilic groups, which bind the water of the retailer, slumped in the middle of the part. The reactions of the sedimentation of the beam are divided into two groups: werewolves (hanging) and non-returning (denaturation).
6) denaturationthe source of the change in the secondary and tertiary structure of the protein is called, so that the system of non-covalent interactions is destroyed, so that the first covalent (primary) structure is not started. The denaturation of proteins relieves any biological activity in the clitin and it is important to vicorate like a lot of amino acids. Denaturing agents can be chemical factor Key words: acids, meadows, hydrating salts, organic oxidizers, various oxidizers. Physical factors can be affected by: high pressure, bagatorase freezing and freezing, ultrasonic fluff, UV radiation, ionizing radiation. Ale, the most wide-spread physical official of the denaturation of the protein of the temperature increase.
In a number of vipadkiv denaturations of proteins in clitiny, there may be renaturations, so that they burn back at the cob expanse of the structure. This process is dependent on the participation of specific proteins, so called bіlkіv thermal shock ( heat shock proteins or hsp) with a molecular weight of 70 kDa. These proteins are synthesized in clitins in a great number of patients with influx on it (or the whole organism) of unfriendly factors, increased temperature. Coming up to the burnt polypeptide lancet hsp 70 Shvidko gortayut її have the correct cob structure.
Classification of whites
For retail: water, salt, alcohol, non-solder and other.
Behind the conformational structure : fibrillar, globular.
For the chemical industry: proteins - are formed only from amino acids, proteins - AA cream can store a non-protein part in storage (carbohydrates, lipids, metals, nucleic acids)
Proteins :
1) Albuminy- Opening by the water, not opening in the conc. salts. R I = 4.6-4.7. Іsnuyut milk albumin, eggs, blood sirovatki.
2) Globulins - do not differ in water, differ in salt. Immunoglobulins.
3) Histones are rare in water, in weakly concentrated acids. Mayut vrazhenі osnovnі vlastivostі. Cenuclear proteins, stench associated with DNA and RNA.
4) Scleroproteins - proteins of supporting tissues (cartilage, brushes), skin, hair. Do not differ in water, weak acids and meadows.
A) collagen- fibrillar proteins of a happy tissue. At a thriving boil, the stinks disperse in the water, and at a cold, gelatin settles.
b) elastin - proteins of ligaments and tendons. For dominance, they are similar to collagens, ale hydrolysis under the action of enzymes in grass juice;
c) keratin - to enter the warehouse of hair, pіr'ya, saves;
G) fibroin- Bіlok shovku, at the warehouse to mіstit rich serine;
e) prolamins and glutenins - proteins of dewy growth.
Proteides
Krіm AK to revenge the prosthetic group and in the fallow, due to its chemical nature, the stench is classified as:
1) Nucleoproteins - prosthetic group - nucleic acids. Among the numerous classes of nucleoproteins, the most numerous are ribosomes, which are made up of a number of RNA molecules and ribosomal proteins, and chromatin is the main nucleoprotein of eukaryotic clitins, which is made up of DNA and structure-forming proteins – histones (located in the clitin nucleus and head mitochondria). i "Matrix Biosynthesis").
2) Hemoproteins - a non-protein component of these proteins - heme, promptings from chotyrox pyrolytic cells, with them binding a bivalent ion (through nitrogen atoms). To such proteins lie: hemoglobin, myoglobin, cytochromes. This class of proteins is called chromoproteins, heme shards are made with a farbowed half. Hemoglobin- Transport sour. Myoglobin - storage of sour in m'yazakh. Cytochrome(enzymes) – catalysis of oxide reactions and electron transport in the dichal lance.
(Report div. appendix 1).
3) Metal proteins - metal enters the warehouse of the prosthetic group. Chlorophyll- To avenge the gem, but to replace the hall - magnesium. Cytochrome a - revenge for mid, succinate dehydrogenase and in. enzymes to fight non-geminic acid ( ferrodoxin).
4) Lipoproteins - to avenge lipids that enter the warehouse of cellular membranes
5) Phosphoproteins - to remove excess phosphoric acid
6) Glucoproteins - revenge tsukra
LITERATURE BEFORE ROZDILU IV.2.
1. Balezin S. A. Workshop on physical and colloidal chemistry // M:. Osvita, 1972, 278 p.;
2. Bishevsky A. Sh., Tersenov O. A. Biochemistry for a doctor // Yekaterinburg: Uralsky robotnik, 1994, 384 p.;
3. Knorre D. G., Mizina S. D. Biological chemistry. - M.: Vishch. school 1998, 479 pp.;
4. Molecular biology. Structure and functions of proteins / Ed. A. S. Spirina // M.: Vishch. school, 1996, 335 p.;
6. Ravich - Shcherbo M. I., Novikov V. V. Physical and column chemistry // M:. Visch. school, 1975.255 p.;
7. Pilipovich Yu. B., Egorova T. A., Sevastyanova G. A. Workshop on global biochemistry // M.: Prosvitnitstvo, 1982, 311 pp.;
Amino acids The warehouse of natural polypeptides and proteins includes amino acids, in the molecules of which amino and carboxyl groups are linked with one and the same carbon atom. H 2 N–CH–COOH R Natural amino acids are subdivided into aliphatic, aromatic heterocyclic ones as a source of water and carbohydrate radical R. Aliphatic amino acids can be non-polar (hydrophobic), polar uncharged and polar charged. In addition to the functional groups in the radicals, there are also amino acids that can be replaced by hydroxyl, amide, carboxyl and amino groups. Sound vikoristovuyutsya trivial names of amino acids, like povyazanі z dzherelami їkh vіdіlennya chi dominion.
Classification of -amino acids for the bodovoy carbohydrate radical Aliphatic non-polar radical H-CH-COOH NH 2 CH 3 -CH-COOH glycine NH 2 CH 3 CH -CH-COOH CH 3 NH 2 alanine CH 3 CH CH 2-CH-COOH CH 2 CH –CH–COOH H 3 C NH 2 isoleucine NH 2 leucine Aliphatic polar radical CH 2 –CH–COOH BIN NH 2 HS–CH 2 –CH–COOH CH 3 CH –CH–COOH serine BIN NH 2 CH 2 – CH–COOH NH 2 cysteine threonine SCH 3 NH 2 methionine CH 2 CH 2 –CH–COOH CH 2 –– CH–COOH CONH 2 NH 2 glutamine COOH NH 2 aspartic acid NH 2 glutamic acid CH 2 2 lysine CH 2 –– CH–COOH H 2 N–C–NH–CH 2 –CH–COOH NH CONH 2 NH 2 asparagine NH 2 arginine Aromatic heterocyclic radicals ––CH–CH–COOH Heterocyclic radical –CH–COOHHO – –CH–COOH HN N NH COOH Carbocyclic radical tyrosine NH phenylalanine NH 2 2 2 histidine N–H proline
Replaceable and non-replaceable -amino acids All natural amino acids can be divided into non-replaceable ones, which are present in the body only from the outermost medium, and substitutions, the synthesis of which are found in the body. Essential amino acids: Essential amino acids: valine, leucine, isoleucine, glycine, alanine, proline, lysine, methionine, threonine, serine, cysteine, arginine, histidine, tryptophan, phenylalanine asparagine, glutam іn, aspartic acid can act as other amino acids, as well as speech, which belong to other classes of organic compounds (for example, keto acids). The catalysts and participants in this process are enzymes. Analysis of the amino acid warehouse of various proteins shows that the proportion of dicarboxylic acids and iogo amides in most proteins is 25-27% of all amino acids. Together with leucine and lysine, the amino acids themselves form approximately 50% of all amino acids of the protein. At the same time, a part of such amino acids, such as cysteine, methionine, tryptophan, histidine, is brought to more than 1.5 - 3.5%.
Stereoisomeria of -amino acids Expansive or stereoisomeric or optically active spoluki - spoluki, zdatnі іsnuvati vzglyadі dvh іsomerіv, є є dlіzornymі vіbrazhennyam druzhny (enantiomer). All-amino acids, cream glycine, optically active half-shells and building wraps the polarization plane of a plane-polarized light (all the winds are swayed in the same plane) to the right (+, right-hand wrapping) or to the left (-, left-hand wrapping). Signs of optical activity: - The presence in the molecule of an asymmetric carbon atom (an atom tied to a chortir by various intercessors); - Visibility in the molecule of the elements in symmetry. The enantiomers of -amino acids look like they have a clear configuration and are called D, L-nomenclature.
Remarkable configurations of -amino acids In the alanine molecule, another carbon atom is asymmetric (there are 4 different intercessors: the atom is water, carboxyl, methyl and amino groups. group atom linked to an asymmetric atom i 3 L-alanine ino acids. wrapping of the polarization plane of plane polarized light (Phenylalanine, tryptophan, leucine etc.)
The configuration of amino acids indicates the space structure and biological power of the amino acids themselves, biopolymers - proteins, as a result of excess amino acids. For certain amino acids, there is a link between their configuration and taste, for example, L Trp, L Fen, L Tyr, L Lei may have a hot taste, and їx D enantiomers of licorice. The licorice taste of glycine has been around for a long time. The L isomer of threonine tastes sour to some people, hot to others. Monosodium sil glutamic acid and sodium glutamate one of the most important noses savory yakos scho zastosovuyutsya at the food industry. Please respect that, similarly to the dipeptide s aspartic acid and phenylalanine, it produces an intensely licorice relish. All amino acids are crystalline speech, which can be even higher than the temperature of the rule (over 230 ° C). Most acids are good in water and practically do not differ in alcohol and diethyl ether. Tse, yak and high melting temperature, testify about the salt-like nature of these rivers. The specificity of amino acids is determined by the presence in the molecules of the amino group (basic character) and the carboxyl group (acid power), which leads to amphoteric electrolytes (ampholytes).
Acid-base power of -amino acids In amino acids, both the acidic carboxyl group and the basic amino group are present at the same time. In water varieties and solid state, amino acids are found only in internal salts - a few ions or bipolar ions. Acid-base ratio for amino acids can be described: CH 3 -CH-COO - BIN - NH 2 H + anion CH 3 -CH-COO - H + + NH 3 bipolar OH- ion CH 3 -CH-COOH + NH 3 cation B the acid medium of the amino acid molecule is the cation. When missed electric struma through such a gap, the cations of amino acids collapse to the cathode and are renewed there. In the puddle middle, amino acid molecules are anion. When an electric stream is passed through such a gap, the anions of amino acids collapse to the anode and are oxidized there. Value of people H, when practically all amino acid molecules are called bipolar ion isoelectric point (p. I). Which one has a significant r. H rozchin amino acids do not conduct an electric struma.
p value I most important α-amino acids Cysteine (Cys) Asparagine (Asp) Phenylalanine (Phe) Threonine (Thr) Glutamine (Gln) Serine (Ser) Tyrosine (Tyr) Methionine (Met) Tryptophan (Trp) Alanine (Ala) Valine (Val) Glycine (Gly) Leucine (Leu) Isoleucine (Ile) Proline (Pro) 5, 0 5, 4 5, 5 5, 6 5, 7 5, 8 5, 9 6, 0 6, 1 6, 3 Aspartic acid (Asp) Glutamic acid (Glu) Histidine (His) Lysine (Lys) Arginine (Arg) 3.0 3.2 7.6 9.8 10.8
Chemical power of -amino acids Reactions for the participation of the carboxyl group Reactions for the participation of the amino group Reactions for the participation of the carbohydrate radical of the acid Reactions for the participation of the carboxyl and amino groups
Reactions for the participation of the carboxyl group -amino acids Amino acids can enter into the same chemical reactions and give the same similar effects as other carboxylic acids. CH 3 -CH-COOH Na. OH CH 3 -CH-COONa NH 2 CH 3 -CH-COOH NH 2 CH 3 BIN NH 3 NH 2 t NH 2 CH 3 -CH-CONH 2 NH 2 alanine amide One of the most important reactions in the body is the decarboxylation of amino acids. With the addition of CO 2 to the decarboxylases, the amino acids are converted into amines: CH 2 –CH–COOH NH 2 glutamic acid + H 2 O methyl ester alanine CH 3 –CH–COO– NH 4+ NH 2 CH 3 –CH–CO H + CH 3 -CH-COOH + H 2 O sodium strength alanine CH 2 -CH 2 NH 2 -CO 2 -aminobutyric acid (GABA) acts as a neurotransmitter COOH COOH NH 2 phenylalanine [O] HO– –CH 2 –CH–COOH NH 2 tyrosine
Reactions for the participation of amino groups -amino acids As well as other aliphatic amines, amino acids can react with acids, anhydrides and acid chlorides, nitrous acid. CH 3 –CH–COOH HCl CH 3 –CH–COOH NH 2 +NH CH 3 –CH–COOH NH 2 CH 3 COCl –HCl CH 33–CH–COOH CH –CH–COOH 3 Cl– alanine chloride CH 3 –CH -COOH NH-CO-CH 3 HNO 22 HNO acid 2 -acetylaminopropanoic CH 33-CH-COOH CH -CH-COOH + N 22+ H 22 O + N + HO OH 2 -hydroxypropanoic acid NH 22 NH When heated amino acids intermolecular dehydration for the participation of both amino and carboxyl groups As a result, cyclic diketopiperazine is established. 2 CH 3 –CH–COOH NH 2 t – 2 H 2 Pro CH 3 –CH–CO–NH HN––CO–CH–CH 3 diketopiperazine alanine
Reactions for the participation of amino groups -amino acids Deamination reactions. oxidative deamination CH 3 -CH-COOH [O] NH 2 CH 3 -C - COOH + NH 3 pyruvic O acid double deamination CH 3 -CH-COOH [H] NH 2 CH 3 -CH 2 - COOH propanoic acid + NH hydrolytic deamination of CH 3 -CH-COOH NH 2 H 2 Pro CH 3 -CH-COOH lactic HO acid + NH 3 intramolecular deamination of CH 3 -CH-COOH NH 2 CH 2 \u003d CH - COOH propenoic acid + NH 3 CH–COOH NH 2 HOOC–CH 2–C – COOH + ketoglutaric acid O CH 3 –C–COOH O HOOC–CH 2–CH–COOH NH 2
The dissolution of the peptide linkage Amino and carboxyl groups of amino acids can react one by one without the dissolution of the cycle: H 2 N –CH–COOH + H 2 N –CH–COOH CH 3 CH 2 OH H 2 N –CH–CO–NH – CH– COOH –H 2 O CH 3 CH 2 OH dipeptide alanine serine alanilserine Vinicaje in the case of –CO–NH– linkages is called a peptide linkage, and the product of amino acid interaction is called a peptide. As a result, 2 amino acids entered the reaction, a dipeptide was released; 3 amino acids – tripeptide thinly. bud. Peptides with a molecular weight of more than 10,000 trochi are called oligopeptides, and those with a molecular weight of more than 10,000 are called polypeptides, or proteins. Peptide links in the warehouse of peptides due to their chemical nature are amides. Polypeptide lances are made up of cells that are regularly repeated, making up the backbone of the molecule, and variable cells - biological radicals and amino acid residues. The cob of polypeptide lancet is treated with a term that carries a strong amino group (N term), and the polypeptide lance is terminated with a viable carboxyl group (C term). Name the peptide, sequentially reordering, starting from N endings, name the amino acids that go up to the peptide; at any time, the suffix “in” should be replaced by the suffix “mul” for all amino acids, krim kіntsevoy. To describe the future peptides, it is not necessary to use traditional structural formulas, but rather short definitions that allow compact writing. H 2 N -CH-CONH -CH-CONH -CH 2-CONH -CH-COOH CH 2 SH CH 3 CH (CH 3) 2 CH 2 OH
In this hour, the most profound is the polypeptide theory of the future protein molecule. Proteins can be classified: - according to the shape of the molecules (globular and fibrillar); - by molecular weight (low and high molecular weight); - behind a warehouse or a chemical warehouse (simple and folding); - for the functions that are counted; - By localization in the clitin (nuclear, cytoplasmic and in); - According to localization in the body (blood proteins, liver and other); - according to the ability to adaptively regulate the quantity of these proteins: proteins that are synthesized with constant susceptibility (constitutive); - for the trivality of life in the clitin (when the days are changed quickly, the days are changed less than 1 year, until the day the days are changed more often, the period of the days when they are changed is calculated in days and months); - According to similar villages of the primary structure and disputed functions (birthplaces of whites).
Functions of the protein Function of the protein Catalytic (enzymatic) Transport Structural (plastic) Short-term Regulatory (hormonal) Zahisn Energetic Daily Application Accelerated chemical reactions Pepsin, trypsin, in the body catalase, cytochrome oxidase Colagen, elasticity tissue keratin Regulation of the exchange of speech in insulin, somatotropin, clitin and tissues glucagon, corticotropin Protection of the body in the form of interferon, ear stimulating factors, immunoglobulin
Classification of the simplest proteins of Albumin. Approximately 75-80% of the osmotic pressure of blood serum proteins falls on albumin; Another function is the transport of fatty acids. The globulins are found in the blood in the complex with bilirubin and high-gauge lipoproteins. The fraction of β globulin includes prothrombin, which is a precursor of thrombin protein, which is responsible for the transformation of blood fibrinogen into fibrin during blood glottis. Globulins win their function. Protamines are low molecular weight proteins, which may show the main power, zoom in their presence in 60 to 85% arginine. In nuclei, clitins are associated with DNA. Histones are small proteins of the main character. The stock includes lysine and arginine (20-30%). Histones play an important role in the regulation of gene expression. Prolaminated whites of the dewy field, are mainly found in native cereals. All proteins of this group during hydrolysis give a significant amount of proline. Prolaminum should be treated with 20-25% glutamic acid and 10-15% proline. The most important sources are orizenin (from rice), glutenin (from wheat), zein (from corn), and other. Glutelin is a simple protein, it can be found in our cereals, in the green parts of the roslin. For glutelins, it is typical to have a high content of glutamic acid and the presence of lysine. Glutelins are storage proteins.
Classification of foldable proteins Class name Nucleoproteins Prosthetic group Prefabricated half-shells (hemoproteins, flavoproteins) Nucleic acids Phosphoproteins Phosphoric acid Chromoproteins Metaloproteins Metal ions Glycoproteins Lipoproteins Bcarbohydrates Milk casein, ovalbumin, vithelin, ichthulin Ferritin, transferrin, ceruloplasmin, hemosiderin Glycophorin, interferon, immunoglobulins , mucin
The primary structure of the protein is the sequence of amino acid dispersal in the polypeptide lanciug. Її signify, successively adding amino acids in the form of protein by way of hydrolysis. For the splitting of N cincic amino acid, the proteins are treated with 2, 4 ditrofluorobenzene, and after acid hydrolysis, only one N cincic acid appears bound to the cym reagent (Sanger's method). Following the Edman method, in the process of hydrolysis, N cincic acid is hydrolyzed in the form of a product of interaction with phenylisothiocyanate. For the purpose of cincemic acid, vicarious hydrolysis is called for in the presence of a special enzyme - carboxypeptidase, which opens the peptide linkage from that peptide, deleting the free carboxyl group. Іsnuyut i khіmіchnі methods and splitting of cincic acid, for example with vicarious hydrazine (Akaborі's method).
The secondary structure of the protein is a way of packing an arched polypeptide lancet - a spiral or a folded conformation. Coils of the helix or folds are trimmed, mainly due to additional intramolecular bonds, which are blamed between the water atom (in the warehouse -NH or -COOH group) of one coil of the helix, or the folds and the electronegative atom (oxygen or nitrogen) of the suture coil a more folds.
The tretinous structure of the protein The tretinous structure of the protein is a trivi- merous space orientation of the polypeptide helix of the folded structure in the syllable obsession. Distinguish between globular (kulyastu) and fibrillar (tightened, fibrous) tertiary structures. The retinal structure is formed automatically, spontaneously, and is again recognized as the primary structure of the protein. In this case, the interactions involve the bichni radicals of amino acid residues. Stabilization of the tertiary structure is due to the balance between amino acid radicals of water, ionic, disulfide bonds, as well as van der Waals forces of gravity between non-polar carbohydrate radicals.
Scheme of the establishment of bonds between amino acid radicals 1 - ionic bonds, 2 - water bonds, 3 - hydrophobic interactions, 4 - disulfide bonds
The quaternary structure of the protein The quaternary structure of the protein is a way of laying in the space of four polypeptide lancets and molding structurally and functionally a single macromolecular light. The molecule, which has settled down, is called an oligomer, and other polypeptide lances, from which veins are composed - protomirs, monomers or subunits (they are called pairs of numbers: 2, 4, or more 6 or 8). For example, a hemoglobin molecule is composed of two - that two - polypeptide lances. The skin polypeptide lanciug has a heme group - a non-protein pigment, which gives the blood a red color. At the warehouse of the gem itself there is a cation of salvage, building and transporting oxygen necessary for the functioning of the body. Hemoglobin tetramer The quaternary structure may be close to 5% of proteins, including hemoglobin, immunoglobulin, insulin, feritin, and may be all DNA and RNA polymerase. Hexamer insulin
Color reactions for the detection of proteins and amino acids For the identification of peptides, proteins and other amino acids, vicory is called “color reactions”. A universal reaction to the peptide group is the appearance of a red-violet infection when the ionic protein in midi (II) is added to the level in the puddle medium (biuret reaction). The reaction to the excess of aromatic amino acids - tyrosine and phenylalanine - the appearance of a yellow infection during the analysis of the distribution of the protein with concentrated nitric acid (xanthoprotein reaction). Give sirkovisnі proteins to black farbuvanni when heated with pink lead(II) acetate in puddle medium (Fol's reaction). Severe acid reaction of amino acids - the adoption of blue-violet fermentation with interaction with nindrine. Proteins should also be given to Ningidrin reaction.
The significance of proteins and peptides Proteins form the material basis of the chemical activity of cells. Functions of proteins in nature are universal. Among them are enzymes, hormones, structural (keratin, fibroin, collagen), transport (hemoglobin, myoglobin), rukhovi (actin, myosin), storage (immunoglobulins), storage (casein, ovalbumin) proteins, toxins (smear, toxin ). In the biological plan, peptides are distinguished by a wide range of functions in proteins. The most characteristic of peptides is the regulatory function (hormones, antibiotics, toxins, inhibitors and enzyme activators, transporters of ions across membranes). Recently, a group of peptides in the brain - neuropeptides - was introduced. The stench is poured into the processes of learning that memory, regulating sleep, and inducing an analgesic function; prostezhuetsya zv'yazyok deyakih neuro-psychic ailments such as schizophrenia, and from instead of quiet chi іnshih peptides in the brain. In this hour, success has been achieved in the elimination of the problem of the spivvіdnennia of the structure and functions of proteins, the mechanism of their participation in the most important processes of the life of the organism, the understanding of the molecular foundations of the pathogenesis of ailments. Prior to actual problems lie the chemical synthesis of protein. Otrimanya synthetic way analogs of natural peptides and proteins in the poklikan to accept the virishhenny of such nutrition, as a mechanism for the development of spoluk in clitiny, the establishment of an interrelationship between their activity and the spacious budovaya, the creation of new medicinal products that food product, and also allows you to go to the modeling of processes that take place in the body.
Deshcho tsіkave about proteins Proteins are the basis of various biological adhesives. So, the trappings of spiders are formed mainly from fibroin - protein, which is seen as spider warts. Tsya syrup-like viscosity of speech is harder on the surface, transforming into mіtsna and indistinct thread at the water. Shovkoviny, which makes the spiral thread of the cobweb, sweep the glue, which eliminates the appearance of the boot. The spider itself is free with radial threads. Zavdyaki special adhesives flies and komakhi zdatnі vyyavlyat simply a diva of acrobatics. Blizzards glue their eggs to the leaves of the trees, and if you see swifts, nests will be made from striking visions. sly vines, sturgeon caviar on the bottom stone. Deyakі see rablikiv for the winter, or in the period of dryness they put shells on a special “door”, like the rablik itself is brought from a sticky, hard protein, so it’s easy to take revenge. Vіdgorodivsya vіd zvnіshny svіtu drench with a hard membrane, rablik crosses the unfriendly hours in the shell. If the situation changes, you just get over it and stop living like a self. Sticky speeches, with which the inhabitants of the water are crusted, can be caught under the water. To that warehouse, there is a small amount of different proteins, which allow water to interact with each other with the approved micaceous glue. Glue, like medium sticks to the stone, does not differ in water and double epoxy resin. Nine cey protein is synthesized in laboratory minds. The majority of sticky speeches cannot be tolerated by vologists, and the white glue of mussels can be used to glue brushes and teeth. This protein does not cause toxic reactions by the body, which is even more important for medical preparations.
Descho tsіkave about proteins Methyl ether L aspartyl L phenylalanine has a licorice relish. CH 3 OOS-CH (CH 2 Z 6 H 5) -NH-CO-CH (NH 2) -CH 2-COOH. Speech vіdoma under the trade name "aspartame". Aspartame is not only malty for zukor (in 100-150 times), but it has a strong licorice relish, especially in the presence of citric acid. Licorice and richly similar apartments. Z yagid Dioscoreophylum cumminsii (the Russian name is not known), found among non-Nigerians in 1895, monelin protein was seen, which was malted for zukor 1500 - 2000 times. Even stronger - in 4000 times - having overturned sucrose protein thaumatin, visions of brightly red fleshy fruits of the African bush Thaumatococcus daniellii. The intensity of licorice relish of thaumatin grows even more when the protein interacts with aluminum ions. Utvoreniya complex, which otrimav trade name talin, malted sucrose in 35,000 times; if you don’t match the mass of talin and sucrose, but the quantity of their molecules, then talin will appear malted 200 thousand times already! Another more licorice protein is a miraculin of visions of the past century from the red fruits of the chagar tree Synsepalum dulcificum daniellii, which they called “miraculous”: a person who chewed on these fruits changes tastes. So, in otstu, there is a welcome wine relish, lemon juice transforms into a licorice drink, and the effect is three times a day. As soon as all exotic fruits are grown on plantations, the local industry will have fewer problems with transporting products. Aje, a small piece of thaumatin can be replaced by a whole bear of succulent dog! On the cob of the 1970s, the sound was synthesized, the best of all syntheses. Ce dipeptide, prompted by the excess of two amino acids - aspartic and aminomalonic. The dipeptide and two carboxyl groups have an excess of aminomalonic acid replaced by a folding fiber group, saturated with methanol and fenchol (wine ethereal oliya roslin and look like turpentine). Tsya speech is approximately 33,000 times malt for sucrose. So that a bar of chocolate has become a resounding licorice, enough of a few milligrams of spices.
Descho tsіkave about proteins Khimіchni ta Physical power shkiri and hair are determined by the power of keratins. In the skin type of creatures, keratin may have some special features, so the word lives in multiple. KERATINI - indistinct proteins of the backbone in the water, which make up the hair, wool, horny ball of shkiri, nails. Under dee, water the keratin skins, hair, nails grow, swell, and after the vaporization, the water becomes harder again. The main chemical feature of keratin is that it contains up to 15% amino acids in order to avenge cysteine. Atoms of the ring, present in the cysteine part of the keratin molecule, easily form bonds with the atoms of the ring of the susceptible molecule, vitiate the disulfide sites, thus linking the macromolecules. Keratins are visible to fibrillar whites. In textiles, stench is found in seemingly long threads - fibrils, in which molecules are woven in bundles, straightened into one bead. In these threads, there are macromolecules connected with each other chemical bonds(Fig. 1). Spiral threads are twisted into a triple spiral, and 11 spirals are combined with microfiber, so as to become the central part of the hair (div. Fig. 2). Microfibrils combine into macrofibrils. a) Aqueous b) Ionic c) Non-polar d) Disulfide Mal. 2. Hair keratin - fibrous protein. zv'yazku zv'yazku vzaєmodії ny places Small. 1. Types of interactions between lanceolate protein molecules
Deshcho tsіkave pro squirrels Hair may have a heterogeneous structure in the transverse section. From the point of view of chemistry, all balls of hair are identical and are formed from one chemical layer - keratin. Ale in the fallow stage and type of structure of keratin is used to develop balls with different authorities: the cuticle is a superficial luscious ball; fibrous, or kirk ball; core. The cuticle is closed with flat cleats, which overlap each other like a ribbed luska. From a glance of cosmetics, the most important ball is hairy. I’ll lie down on my own old look hairy: glare, springiness or, navpaki, darkness, posichenity. The cuticle mill is poured into the process of farbuvannya hair and curling, so for the penetration of the preparations in the globular balls hair, to the pigment, it is necessary to soften the cuticle. Keratin, from which “little patches” are formed, swells under the effect of water, especially as it is accompanied by the effect of heat and other preparations (cute). From a glance of chemistry, it is explained by the development of water bonds in keratin molecules, which, when hanging, hairs are restored. When the shawls are swollen, the edges of them stand up vertically, the hair shines. Razm'yakshennya cuticles change the mechanical strength of the hair: it's easier to mess with the hairy man. Spread between the edges of the small patches of coverings with silk fat, which gives the hair shine, softness, elasticity. Fibrous, abo kirkovy, a ball of creations with long spindle-like cornified clitins, ruffled in one straight line; in a new place, the elasticity and springiness of the hair. In this ball, there is a melanin pigment, which is consistent with the color of the hair. Zabarvlennya volossa lie down due to the presence in the new melanin and the bulbs again. Light hair to avenge the rosy pigment, dark - granular. The core, or the ball of the brain, is composed of not overly cornified clitin.
Subject:Proteins - natural biopolymers
“Changing the skin to wash your image of vibes,
capricious, like a child, and primary, like dim,
to boil everywhere life in trivozi metushlivoy,
great zmishavshi with worthless and ridiculous ... "
S.Ya. Nadson
| Methodical information |
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| Occupation type | Integration (biology + chemistry) problematic multimedia lesson |
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| To form statements about the power and functions of proteins in cells and organisms |
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| Initial: give understanding about proteins - natural biopolymers, their various functions, chemical power of proteins; to form knowledge about the unique features of the life of the city; destroy knowledge about the relationship between the future and the functions of speeches on the butt of whites; vivchati uchnіv, vykoristannyu knowledge of summіzhnyh obtіvіv otrimannya more povnoї picture of the world. Developing: development of cognitional interest; installation of intersubject links; dodoskonalyuvat vminnya analizuvati, porivnyuvati, establish vzaimozv'yazok mizh budovoi that power. Vikhovny: show the material unity of the organic world; molding the scientific svetoglyadu; |
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| The method of problematic vikladu, chastkovo-poshuk, heuristic, doslidnitsky |
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| Display function: | Learner using a fluke robot, consultant |
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| Knowledge, vminnya, beginners and competencies, as they begin to actualize, wake up, consolidate during the course of employment: | Such rhetorical operations are formed, such as the alignment of the power of the protein, the classification of the structures of the protein molecule, the analysis of the functions of the protein. Basic concepts: Amino acids, peptide linkage, polypeptide, protein structure, protein function, protein power, denaturation. Basic skills: Robot with chemical properties, robot with detection of catalase activity |
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| Required possession of that material: | Computer, presentation on the topic of the lesson. Experiment: test tubes, tripods, spirit lamp, utrivac. Reactive materials: rr Bilka chicken egg, nitric acid, solution for midi(II) sulfate, meadow, 3% water peroxide, orphan boiled potatoes chi m'yaso. |
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| Conducted type of activity: | Productive, Creative, Problematic |
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| Technological employment card |
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| Motivation: | How can you help you with your future profession? |
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| Hid busy: |
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| “Proteins, fats and carbohydrates, |
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| Actualization of knowledge | And chi know Vi: 8. How did the life of the Earth appear? What is the basis of life? The axis of today speaks about meme. Activity plan: Appointment. Functions of whites. Warehouse that Budova Bіlkіv. The structure of proteins. Chemical power of proteins. 6. Reorganization of proteins in organisms. |
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| Food problem? How can Budov's white be tied to him by power and functions? Hypothesis: Apply whites Review history: Warehouse bіlkіv Appointment | It is not easy to understand how proteins can be transferred to other different functions. The only way to get closer to the solution of the problem is to find out why the proteins are motivated, how the structural elements are mixed, how to form the molecule, according to one to one that in space, how the stench interacts one with one with those speeches of dokovillya, that . Vivchiti Budova and the power of Bіlkіv. |
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| Explore the causal and inherited staleness: functions – budova. proteins - polymers, monomers - amino acids |
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| Can you name the proteins for you? globulin - vaccine, rhodopsin - zorovyi purpura, In the middle of the 19th century, a cob of white vines was laid, and after 100 years of aging, squirrels were systematized, a warehouse was designated, and wisps were grown, as squirrels are the main component of living organisms. A Ya. Danilevsky- presence of a peptide bond in the protein E. Fisher- synthesizing half of the protein Chemical warehouse squirrel can be represented by such danims: Z -55%, Pro - 24%, H - 7,3%, N - 19%, S -2,4%. Before bіlkіv be brought more than 50% of the total mass of organic sprouts of brine: in meat - 80%, in skins - 63%, in livers - 57%, in brains - 45%, in brushes -28% Chemical formulas of active proteins: Penicillin С16Н18О4N2 Casein С1864Н3021О576N468 S2 Hemoglobin C3032H4816 O872N780S8Fe4 - Let's define the term BILOK BILKI- biopolymers of irregular budov, monomers such as 20 amino acids different types. At chemical warehouse amino acids include: C, Pro, H, N, S. Protein molecules can make up a wide range of structures and conjure low functions in the body and organism: budwell, catalytic, regulatory, rukhova, transport |
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| Functions of whites | - Proteins- the basis of life on Earth, which enters the warehouse of skin, m'azova and nerve tissue, hair, tendon, walls of the vessels of creatures and people; tse budіvelniy material kіtini. The role of proteins is important to reevaluate, incl. Life on our planet can be deciphered as a way of using protein bodies, as a way of exchanging speech and energy from the outer core. Oskіlki belok to avenge various functional groups, vin can be introduced to any of the earlier developed classes of spoluk. In a new yak, at the focus, there will be signs of spoluk, which lie down to different classes. Zvіdsi yogo rіznomanіttya. Due to the peculiarities of yogo structure, it characterizes the proteins as I see the shape of the development of the speech. |
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| Protein structure | Put together a summary and feedback from the process of roaming for information: Do any excess amino acids enter the warehouse of protein molecules? (div.app.) For the calculation of which functional groups of amino acids are used one by one? What to understand under the primary structure of the protein? What is the "secondary" structure of the protein? Yakі zv'yazki її utrimuyut? What is a "tretin" structure? For rahunok such zv'yazkіv vyutvoryuetsya? Why is the quarter structure peculiar? (Looks like a linear sequence of amino acids)
-What is the primary structure of the protein? How do links stabilize the secondary structure? ( The spacious configuration of the protein molecule is folded like a helix. In molding the spiral configuration of the polypeptide lancet play a role water links mizh-Z=Pro ta -N-H groups. . )
- What is the tretin structure of the protein? (E then the configuration of a seemingly spirally coiled polypeptide lancet. It is supported by the interaction of various functional groups of the polypeptide lanciug. So, between the atoms of the sirka, a disulfide site is established, between the carboxyl and hydroxyl groups it is a collapsible site, and between the carboxyl and amino groups, a salty site can be added. For tsієї structures are characteristic of water links).
- What is the quarter structure of the protein?(Deyakі protein macromolecules can join together one by one and form admirably large aggregates-macromolecules of the protein).
Yaki Chemical power be characteristic for whites? (Amphoteric is associated with the presence in the protein molecule of cationic groups - amino group and anionic - carboxyl groups. The sign of the charge of a molecule to lie in a number of large groups. If the carboxyl groups are more important, then the charge of the molecule is negative (the power of a weak acid is manifested), if the amino group is positive (the main power)).
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| Chemical power of proteins | For whites, reactions are characteristic, for some, there are sieges. But in some cases of lifting sieges, when too much water is used, it breaks up, and in others, it is irrevocably swallowed, tobto. denaturation. Changes in the secondary, tertiary and quarter structures of the protein macromolecule under the influence of external factors: temperature, chemical reagents, mechanical influence. During denaturation, the physical power of the protein changes, the diversity decreases, and biological activity is involved What can denaturation lead to? impaired antigenic sensitivity of the protein; Blocking low immunological reactions; Damage to the exchange of speeches; Inflammation of the mucous membrane is low in the organs of etching (gastritis, colitis); Kameneutvorennya (stones to make a white base). Also for proteins are characteristic: Swallowing whites when heated Precipitation of proteins with salts of important metals and alcohol Proteins burn with nitrogen, carbon dioxide and water, as well as some other rivers. The mountain is accompanied by a characteristic smell of scorched feast. Proteins are rotten (under the influence of putrefactive bacteria), with which methane (CH4), circulatory water (H2S), ammonia (NH3), water and other low molecular weight products are dissolved. Amphotericity Budova AK at the infamous look: NH2-CH-COOH, de R - carbohydrate radical. COOH - carboxyl group /acid power/. NH2 – amino group /basic power/. The process of restoring the protein structure is called renaturation The transformation of proteins in organisms. Proteins їzhі → polypeptides → α-amino acids → proteins to the body |
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| How to get a squirrel according to the date to the water? |
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| Hydrolysis | Protein hydrolysis- ruining the primary structure of the protein with dilution of acids, meadows or enzymes, which leads to the solubility of α-amino acids, from these vins of deposition.
Proteins - Albumosy - Dipeptides - Amino acids |
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| Yaksnі kolorovі reactions to protein | Xanthoprotein reaction- Reaction to aromatic cycles. Protein + HNO3(c) → white siege → zhovte zabarvlennya → orange zabarvlennya + NH3 How, for the help of the xanthoprotein reaction, is it possible to revitalize natural threads in the form of pieces? |
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| Biuret reaction- Reaction to peptide bonds. Protein + Cu(OH)2 → purple variety What is it possible for additional chemistry to solve the problem of deficiency of zhі? The rozhe-violet or purple zabarvlennya will appear more appropriately. Ce reaction to peptide bonds in the folds. In the presence of the diluted Cі in the puddle middle, the atom and nitrogen of the peptide lancet are fermented in the purple color complex with midi (II) ions. Biuret (pokhіdne sechovini) to avenge the CONH group - and to that I give a reaction. |
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| Functions of the protein |
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| homework | One vial unselected milk take 288 mg of calcium. How much milk do you need per day to supply your body with a sufficient amount of that element? Dobova need 800 mg of Ca. (Vіdpovіd. To satisfy the additional consumption of calcium, a grown-up person is obliged to drink 2.7 bottles of milk per day: 800 mg Ca * (1 bottle of milk / 288 Ca) \u003d 2.7 bottles of milk). In a piece of white wheat bread, 0.8 mg of salt. Skilki shmatkіv need to be collected per day for satisfaction of additional consumption in this element. (Additional requirement for the rabbit is 18 mg). (Vіdpovіd. 22.5 pieces) 18 mg: 0.8 = 22.5 |
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| Fixing the woven material Gra "Raise your hand, it's okay" | At the same time, you will vikonuvatimete zavdannya z vyvcheno ї by those who looked at the test. (At the time of rechecking, learners change with their robots and evaluate the work of the susida. Variants of the correct answers on the dosh. - What is the structure of the name? Why? -How can you, for help, show the adopted secondary, tertiary, quarter structures of the protein. For rahunok such zv'yazkіv vzaєmodіy tse vіdbuvaєtsya? And now, for the help of the test, we will check it, as you have mastered the material. Raise your hand to answer "So". 1. Amino acids are included in the warehouse of proteins, which are intertwined with each other with watery bonds (Ні) 2. A peptide link is called a link between a carboxyl group of one amino acid and nitrogen of an amino group of another amino acid. (So) 3. Proteins form the main part organic speeches clitiny. (So) 4.Bilok - monomer. (Hi) 5. The product of hydrolysis of peptide bonds is water. (Hi) 6. Products of hydrolysis of peptide bonds - amino acids. (So) 7. Protein is a macromolecule. (So) 8. Catalysts of cells - grains. (So) 9. Use proteins to carry acid and carbon dioxide. (So) 10. Immunity is not related to proteins. (Hi) |
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| Vislovlyuvannya about life and that protein famous people | “Everywhere, de mi zustrіchaєmo life, mi bachimo, scho vyazanі z like a white body.” F. Engels "Anti-Dyuring" The famous mandriving man and the legacy of nature, Oleksandr Humboldt, is still on the verge of the 19th century, giving such a life: “Life is a way of establishing white bodies, the original moment of such a step-by-step exchange of speeches with a superfluous callous nature; moreover, from the attachment of this exchange of speeches, it is attached to life itself, which leads to the distribution of the protein. Appointment, given by F. Engels at the robot "Anti-Dyuring", allows you to think about it, how modern science is the process of life. “Life is the intertwining of the most complex chemical processes in mutual modality of proteins among themselves with those other speeches.” |
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Addendum No. 1
Functions of whites.
catalytic function
Protein yak enzyme: Enzymes are proteins, which may have catalytic activity, tobto. which will speed up the overshoot of reactions. All enzymes catalyze more than one reaction. Illness that is caused by enzyme deficiency.
Butt: milk is not overexposed (no lactase enzyme); hypovitaminosis (vitamin deficiency)
Determination of enzyme activity in biological motherlands great value for the diagnosis of illness For example, for the activity of enzymes in blood plasma viral hepatitis.
Enzymes vikoristovuyut as a reactive agent for the diagnosis of some diseases.
Enzymes vikoristovuyut іz lіkuvannya deyih ailments. Apply: pancreatin, festal, Lidaza.
Enzymes vikoristovuyut in industry: when preparing non-alcoholic drinks, syrups, canned food, cowbass, smoked meats.
Enzymes vikoristovuyutsya when processing flax, hemp, to help the shkir in the shkiryan industry, the stench enters the warehouse of the right powders.
structural function
Proteins are a structural component of rich proteins. For example, the monomers of actin tubulin are globular, differentiated proteins, and after polymerization they form long threads, from which the cytoskeleton is folded, which allows cells to shape. keratin protein is folded hair, nails, pir'ya ptahіv and deyak_ shells.
Zahisna function
Іsnuє kіlka vidіv zahіsnyh funktsіy blіkіv:
Physical zahist. I take the fate of collagen - protein, which establishes the basis of intercellular speech of good tissues (including bones, cartilage, tendon and deep balls of the skin (dermis)); keratin, to form the basis of horny shields, hair, pir'ya, horns and ing. similar to the epidermis.
Chemist. Binding of toxins with protein molecules can lead to detoxification. Particularly important role in detoxification in humans is played by liver enzymes, which decompose and detoxify or translate them into a rozchinnu form, which will absorb them into the body.
Immune Zachist. Proteins, which enter the blood pool and other biological roots, take part in the infection of the body, both for damage and for the attack of pathogens
Regulatory function
Many processes in the middle cells are regulated by protein molecules, so they serve neither as a source of energy, nor as a vital material for the cells. Qi proteins regulate transcription, translation, and induce the activity of other proteins and others.
The regulatory function of the protein is affected either by the function of enzymatic activity, or the function of specific binding to other molecules, as a rule, is intertwined with these molecules of enzymes.
Signal function
The signal function of whites is the ability of whites to serve as signal speeches, transmitting signals between cells, tissues, organs and other organisms. Often the signaling function is combined with the regulatory one, but the shards of rich internal regulatory proteins also affect the transmission of signals.
The signaling function is controlled by proteins-hormones, cytokines, growth factors and others.
transport function
The butt of transport proteins can be called hemoglobin, which carries acid from the lungs to other tissues and carbon dioxide from tissues to the legs, as well as homologous proteins found in all kingdoms of living organisms.
Spare (reserve) function of whites
Before such proteins, there are so called reserve proteins, as they are stored up as a source of energy and speech in native growths and eggs of creatures; proteins of the tertiary shells of the egg (ovalbumin) and the main protein of milk (casein) also serve as the head rank of the life function. A number of other proteins vikoristovuetsya in the body as a dzherelo amino acids, yakі in their line є protagonists of biologically active speeches, which regulate the process of metabolism.
Receptor function
Protein receptors can reside in the cytoplasm, so they can penetrate into the clitin membrane. One part of the receptor molecule receives a signal, which most often serves as a chemical speech, and in some cases it is light, mechanical action (for example, stretching) and other stimuli. When a signal is injected into a single cell, the molecules of the protein-receptor undergo a conformational change. As a result, the conformation of the other part of the molecule changes, which leads to signal transmission of the other cellular component.
Motor (rotary) function
This class of motor proteins ensures the safety of the organism, for example, the shortness of m'yaziv, including locomotion (myosin), the movement of cells in the middle of the body (for example, amoeboid rux leukocytes), directing internal transport create a presentation
Cody food additives
| E103, E105, E111, E121, E123, E125, E126, E130, E152. |
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| 2. Suspicion | E104, EE122, E141, E150, E171, E173, E180, E241, E477. |
| 3. Unsafe | E102, E110, E120, E124,. E127. |
| 4. Carcinogenic | E131, E210-E217, E240, E330. |
| 5. Declutter the intestines to cry out. | |
| 6. Shkіdlivі for shkіri | |
| 7. What to call for a broken vise | |
| 8. Visipi | |
| 9. Raise cholesterol levels | |
| 10. Call out the disorder of the schlunk | E338 E341, E407, E450, E461 - E466 |
Practical robot
Subject: Chemical power of proteins. Yakіsnі (kolorovі) protein reaction".
Tsіl: Learn about chemical reactions to proteins. Activity of catalase enzyme in living and dead tissues.
"Denaturation of proteins"
Vikonanny order.
Prepare the rozchin of the protein.
Pour 4-5 ml of protein powder into a test tube and heat to a boil.
Appoint change.
Cool the test tubes and dilute them with water.
"Xanthoprotein reaction"
Vikonanny order.
2. Pour 1 ml of octic acid into a test tube.
3. Heat up the test tubes.
4. Cool the sumish and add ammonia to the puddle middle.
5. Appoint changes.
« Biuret reaction»
Vikonanny order.
1. Pour 2-3 ml of protein powder into a test tube.
2. Add 2-3 ml of sodium hydroxide and 1-2 ml of blue vitriol.
3. Appoint changes.
Yakіsnі (colourful)
protein reaction. Follow #2 and #3
Xanthoprotein reaction
Protein + HNO3conc > bright-zhovte farbuvannya
(Showing benzene nuclei)
Biuret reaction
Protein + NaOH+CuSO4 > red-
purple farbuvannya
(Revealing of peptide bonds)
"Proof of the presence of a protein only in living organisms"
Vikonanny order.
1. Test-tubes contain fresh squash potatoes, shmatochkas of gray potatoes,
boiled potatoes.
2. Add 2-3 ml of water peroxide to the skin tube.
3. Appoint changes. (catalase - enzyme protein is seen only in
the presence of molecular water, the difference in water, albumin is burned)
| Dosvid | What did they rob | What did they watch out for | Explanation and visnovki |
| 1. Acid reactions to proteins. | |||
| a) Biuret reaction. | Up to 2 ml of the amount of protein, add the amount of sulfate midi (II) and meadow. | Red-violet farbuvannya. | In case of mutual differences, a complex structure between Cu2+ ions and polypeptides is established. |
| b) Xanthoprotein reaction. | Up to 2 ml of protein, add nitric acid drop by drop to concentrate. | Long live. | Reaction to bring, scho to the warehouse of proteins includes excess aromatic amino acids. |
| 2. Protein denaturation. | Heat the test tube No. 3 from the size of the protein. | In all three of the depressions, there is an irreversible swallowing of protein - denaturation. | When heated, diluted with alcohol, salts of important metals, the secondary and tertiary structures are destroyed and the primary is saved. |
"Life is a way of using white bodies ..." F. Engels
Reference abstract Addendum No. 2- AMPHOTERNITY
Kisle middle = after the type of meadow
[protein]+ + OH- = according to the type of acid
- HYDROLYSIS……ruining the primary structure of the protein to α-amino acids
Yakіsnі reactions
- BIURET REACTION(Recognition of peptide bonds in the protein molecule).
B. + CuSO4 + NaOH → purple
………………………………
- XANTOPROTEIN REACTION(Showing benzene nuclei).
B. + HNO3 → zhovte farbuvannya
- Gorinnya Bilku ………………………..
N2, CO2, H2O - smell of burnt fir
- denaturation - ………………………..
temple t ruination
radioactively modified 2-3 structures
salt of important Me
Proteins ProteinsBILKI- the most important warehouse part of living organisms, which enter the warehouse of skins, horny curves, m'yazovo and nerve tissue.
(simple) (foldable) 
| 1 option | 2 option |
| 1. Before the warehouse of amino acids enter: a) only amino groups b) less carboxyl groups c) amino groups and carboxyl groups d) amino groups and carbonyl groups | 1. Amino acid - speech, the formula is: a) CH3CH2 CONH2 b) NH2COOH c) NH2CH2CH2COOH d) NH2CH2SON |
| 2. Amino acids, which cannot be synthesized in the human body, but can only be found in the same way, are called a) a-amino acids b) kharchovimi c) -amino acids d) irreplaceable | 2. Amino acids - ce a) barrelless light boiling water b) gas important for repeat c) crystal speech of erysipelas color d) barless crystal speech |
| 3. When amino acids interact with meadows and acids, they dissolve: b) collapsible air c) dipeptides d) polypeptides | 3. Adoption of polypeptides depends on the type of reaction: a) polymerization b) polycondensation c) coming d) substitution |
| 4. Formula of 3-aminopropanoic acid: a) NH2CH2COOH b) NH2CH2CH2COOH c) NH2CH2CH2 NH2 d) NH2CH CH2COOH | 4. Acid has the weakest acid power: a) otsova b) chlorine c) aminooctova d) dichloroctova |
| 5. Verify that the amino acid is: a) solid language of molecular life b) crystal speech of ionic life c) rіdini, good rozchinnі by the water d) crystalline speech with low melting points | 5. Amino acids - amphoteric half-shells, shards of stench interact: a) from acids b) from the meadows c) with alcohols d) with acids and lugs |
Vіdpovіdі 1 - C, 2 - D, 3 - A, 4 - B, 5 - B Vіdpovіdі 1 - C, 2 - R, 3 -B, 4 -C, 5 - R
| 1 option | 2 option |
| 1. Specify the name of the protein, which will perform its function: | 1. Specify the name of the protein, which is the enzymatic function: a) hemoglobin; b) oxidase; c) antibodies. |
| 2. Proteins - price ..: a) polysaccharides; b) polypeptide; c) polynucleotides. | 2. The biological power of the protein determines the structure: a) tertiary; b) secondary; c) first. |
| 3. The primary structure of the protein is supported by the linkages: | 3. Secondary protein structure a) ionic; b) peptide; c) vodnevih. |
| 4. Hydrolysis of the protein vikoristovuetsya for: a) possession of amino acids, b) acidic manifestation of protein, c) destruction of the tertiary structure | 4. Proteins respond to reactions: a) denaturation, b) polymerization, c) polycondensation. |
| 5. Amino acids, necessary for inducing protein, are consumed by the body: a) with water b) hedgehog; c) repeat. | 5. Which of the most folding processes: a) microbiological synthesis; b) organic synthesis; c) processing of plant protein. |
Variations: 1 – c, 2 – b, 3 – b, 4 – a, 5 – b. Suggestions: 1 – b, 2 – c, 3 – c. 4 – a, 5 – b.
Protein test
1 . What are the chemical elements to be delivered to the warehouse?
a) coal b) water c) sour d) sulfur e) phosphorus f) nitrogen f) salt g) chlorine
2 . How many amino acids take part in the development of proteins?
a) 30 c) 20 b) 26 d) 10
3 . How many amino acids are essential for humans?
a) 16 b) 10 c) 20 d) 7
4 . As a result of which reaction is the peptide bond formed?
a) hydrolysis reaction c) polycondensation reaction
b) hydration reaction d) all other reactions
5 . Yaka functional group nadaє amino acids - acidic, yaka - puddles of authority? (carboxylic, amino group).
6 . How do the bonds establish the 1st primary, 2nd secondary, 3rd tertiary structures of the protein? Spivvidnesit:
a) covalent c) ionic
b) water; d) such links are daily.
7 ) Designate the structure of the protein molecule:
1. 
2.
Table of types
| Food number | |||||||
| Vіdpovіdі option |
8) Denaturation - purifying the protein to _____________ structures under the direction of ________________, as well as under the direction of various varieties chemical speeches(______,________, salts) that radiation.
9) Hydrolysis - the destruction of the _____________ structure of the protein under the direction of ________________, as well as the aqueous composition of the acids or both.
10) Yakіsnі reactions:
a) Biuretova.
Protein + ___________________________ = _________________________
b) Xanthoprotein.
Protein + ________________________________ = __________________________
11) To establish the viability between proteins and their function in the body. Please, give the following sequence of numbers, which should be given to the letters after the alphabet:
BILKS: FUNCTION:
A) hemoglobin 1) signal
B) enzymes; 2) transport
C) antibodies and antitoxins 3) structural
4) catalytic
5) zahisna
12) Save the value of the whites:
| Functions | Value |
|
| Budivelna | Cloth membranes, coverings of fabrics, wool, pir'ya, mountain, hair, cartilage |
|
| transport | Accumulation and transport in the body of the most important speeches |
|
| Energetic | The stock of amino acids in the development of the body |
|
| Dviguna | Short-lived proteins are the basis of m'azovyh fabrics |
|
| Zahisna | Proteins - antibodies, antitoxins recognize and destroy bacteria and “foreign” speech |
|
| Catalytic | Proteins are natural catalysts (enzymes) |
|
| Signalna | Membrane proteins receive foreign influxes and transmit a signal about them to the middle of the cell |
Question before the briefing:
Bіlok is also called…
What are protein monomers?
How many irreplaceable AKs do you see?
What is the atomic warehouse of bіlkіv?
What kind of link supports the secondary structure?
What is the name of the link that makes the POC?
The secondary structure of the protein molecule in the space is guessing ...
For what kind of interactions do the tretinous structure settle?
Why are proteins brought to the IUD?
What does "protein" mean in Greek translation?
What is "denaturation"?
What is the name of the process of interaction of proteins from H2O?
Formation of new knowledge. Lecture block.
Topic agenda:
1. The role of proteins in organisms, natural dzherela bilkiv.
2. Warehouse and budova bіlkіv.
3. Functions of whites.
4.Physical and chemical power of proteins.
5. Synthesis of proteins.
6. Reorganization of proteins in organisms
3 organic speeches to enter before I live in a cell, Proteins play the most important role. Approximately 50% of clitin mass falls on a portion. Zavdyaki squirrels of the body, having gained the ability to collapse, multiply, grow, conquer the hedgehog, react to the cold weather.
“Life is a way of establishing white bodies, the very moment of such a constant exchange of speeches with a superfluous їx callous nature, moreover, with the attachment of this exchange of speeches, life is attached ilka,” wrote Engels at his office.
Proteins are essential components of food products, stinks enter the warehouse of medicinal products.
Protein is an important component of a human being. The main sources of grub protein: meat, milk, processed meat products, bread, fish, vegetables. The need for the protein is to lie in the vіd vіku, statі, type of activity. In the organism of a healthy person, the balance between the number of proteins that are present and the decay products that are seen is to blame. For the assessment of the protein exchange, an understanding was requested protein balance. In healthy people, people have nitrogen equals, tobto. the amount of nitrogen taken from proteins is equal to the amount of nitrogen. In a young organism, where the accumulation of protein mass, the nitrogen balance will be positive, tobto. The amount of nitrogen that comes in, outweighs the amount of what is introduced into the body. In people of a frail age, and also for some people who fall ill, a negative nitrogen balance is observed. Trivaliy negative balance of nitrogen leads to the death of the organism.
It is necessary to remember that the deacids of amino acids in case of thermal processing, trivial conservation of products can create half-life, which is not acquired by the body, tobto. become "inaccessible". Reduce the price of the protein.
Creatures and growing proteins are acquired by the body differently. For example, proteins of milk, dairy products, eggs will be conquered by 96%, meat and ribi - by 93-95%, bread proteins - by 62-86%, vegetables - by 80%, potatoes and legumes - by 70%. However, the sum of these products can be greater in total.
The technology of cultivating food products and yogo culinary processing is pouring into the stage assimilated by the body of proteins. With the moderate heating of grubs, especially the dewy season, the assimilation of whites is growing. For іntensive thermal processing, the penetration decreases.
The supplementary requirement of a mature person in a protein of a different species is 1–1.5 g per 1 kg of body mass, tobto. approximately 85-100 g.
2. Budova bіlkіv.
A lot of organic shelves, which enter the warehouse of cells, are characterized by large sizes of molecules. What are the names of such molecules? (macromolecules) The stench is composed of similar low molecular weight shells, bound together by covalent bonds. You can match the thread with the beads on the thread. What are the names of warehouse elements? (Monomiri). The stench makes polymers. Most of the polymers were induced from the same monomers. Such monomers are called regular. For example, if A is a monomer, then -A-A-A-…….A-polymer. Polymers, among some monomers, are called irregular. For example, -A-B-R-P-A-……G-R-P-A-. Warehouse signifies their power.
Proteins are irregular polymers, monomers of which are amino acids.
Proteins are complex high-molecular natural compounds, stimulated by amino acids. The stock of proteins includes 20 different amino acids, which show the greatest difference in proteins with different combinations of amino acids. As from 33 letters of the alphabet, we can add up an inexhaustible number of words, so from 20 amino acids - an impersonal number. There are up to 100,000 proteins in the human body.
The warehouse of more proteins includes 300-500 amino acid deposits, and more proteins, which add up to 1500 and more amino acids. Proteins are differentiated by the warehouse of amino acids and the number of amino acid lanks, and especially by the order of numbering in polypeptide lances. Rozrahunok show, ShO for BILKA, motivated to 20 riznikh amino acids, pijezi from Lantsyuzi 100 amino acids Zalishkiv, the number of yanging warts is 10130. Bagato bilkiv Great for Dovzhina, I Molecular Mass.
Insulin -5700
Ribonuclease -12700
Albumin-36000
Hemoglobin-65000
Whites are guilty buti for such a mass with long threads. All macromolecules form the formula of compact spools (globules) and twisted structures (fibrils).
Proteins are subdivided into proteins (simple proteins) and proteins (folding proteins). The number of amino acid residues that are included in the molecule, in different ways, for example: insulin - 51, myoglobin - 140. The number of Mr. protein is from 10,000 to ten thousand million.
The first hypothesis about the future protein molecule was proponated in the 70s of the 19th century. Tse bula ureidna theory of life protein. In 1903 p. The German teachings of E.G.Fischer, propagating the peptide theory, became the key to the mystery of the protein. Fischer admitted that proteins are polymers with excess amino acids linked by a peptide bond NH-CO. The idea of the fact that proteins are the only polymers to enlighten, was discussed as early as 1888. Russian scientist A.Ya.Danilevsky. This theory took away the confirmation from the upcoming robots. Possibly to the polypeptide theory, proteins can change the structure
A lot of whites are composed of a number of polypeptide particles, which are folded into a single aggregate. Thus, the hemoglobin molecule (С738Н1166S2Fe4O208) is composed of four subunits. Significantly, Mr egg white = 36000, Mr meat protein = 1500000.
The primary structure of the protein- The sequence of drawing amino acid residues, due to the rahunok of peptide (amide) bonds, all bonds are covalent, mimic.
secondary structure- The shape of the polypeptide lanceug in space. White lance of twists at the spiral, zdіysnyuєtsya for rahunok of impersonal watery zv'yazkіv.
Tretinna structure– a real trivi- mer configuration, which takes on a twisted spiral Tretin structure – a tangle of polypeptide helix. (Demonstration of a ball of elastic cord).
It is easy to reveal the configuration, it is more important to understand, like the forces of її podtrimuyut. (Water bonds, disulfide spots -S-S-, folding link between radicals. zavdyaki forces of van der Waals .) (for rahunok hydrophobic zv'yazkіv), for some proteins - S-S-zv'yazku (bіsulfіdnі mіstki), foldable fіrnі mіstki.
Quaternary structure- One-by-one protein macromolecules are obtained to form a complex. Quaternary structure - structure of several polypeptide lances
Students, graduate students, young adults, like victorious base of knowledge in their trained robots, will be your best friend.
Placed on http://www.website/
1. Ailments, zooming in on impaired synthesis of the functioning of proteins
Proteins є khіmіchnimi spolukami, dіyalnіst yakіh vede before forming normal signs of a healthy organism. Involved in the synthesis of a different protein and a change in its structure leading to molding pathological signs that rose ailment. We call it a sprat of illness, mindful of the damage to the structure and the intensity of the synthesis of proteins.
Classical hemophilia is associated with the presence in the plasma of one of the proteins that take part in the pharyngeal blood; sick people are prone to increased bleeding
Sickle cell anemia is caused by a change in the primary structure of hemoglobin: in sick people, erythrocytes may have a sickle shape, the number of erythrocytes is changed due to the accelerated process of their collapse; hemoglobin zv'yazuє ta endure less, lower at normі, kіlkіst sour.
Gigantism of delusions inspired by the growth hormone; sickness may be over the world at the height of growth.
Daltonism of enchantment in the pigment of the color flasks, which takes part in the molding of the color spray; Colorblind people do not distinguish between colors.
Diabetes is associated with the so-called deficiency of the hormone insulin, which may be due to various reasons: a change in the number of or a change in insulin, as seen, a change in the number or a change in the structure of the insulin receptor inu. In sick people, there is an increase in the amount of glucose in the blood, and accompanying pathological signs develop.
Evil cholesterolemia is bound by the presence in the cytoplasmic membrane of cells of a normal receptor protein, which accepts a transport protein that can carry cholesterol molecules; in the organisms of ailments, cholesterol, which is necessary for clitin, does not penetrate in clitin, and large amounts accumulate in the blood, deposited in the walls of blood-bearing vessels, which leads to their ringing and rapid development of hypertension in early age.
Progressive xeroderma is stunned by disruption of robotic enzymes, which normally renew DNA in cells, which are conditioned by UV-changes; ailments that are impromptu to light, the shards in the minds of the stench blame the numerical shkirnі vrazki and inflamed.
8. Mucoscidosis of the changes in the primary structure of the protein, which forms a channel for ions of SG in the outer plasma membrane; in ailments in the paths of the wounded, a large amount of mucus is accumulated, which leads to the development of diseases of the organs of the respiratory system.
2. Proteomics
The 20th century, which has passed, was characterized by the vindication and the turbulent development of scientific disciplines, as they articulated the biological phenomenon in the warehouses of its components and tried to explain the phenomena of life through the description of the power of molecules, we are ahead of biopolymers, which are included in the warehouse of living organisms. These sciences included biochemistry, biophysics, molecular biology, molecular genetics, virology, biology, bioorganic chemistry. They develop directly in science, as if swaying, from the powers of warehouses, to give a complete picture of the whole biological phenomenon. For the purpose of a new integrative strategy for the knowledge of life, a great deal of additional information is needed. The sciences of the new century - genomics, proteomics and bioinformatics have already begun to submit material for it.
Genomics is a discipline that develops the structure and mechanism of the functioning of the genome in living systems. Genome- Sukupnіst vsіh genіv і mizhgennih dolyanok be-any organism. Structural genomics of living genes and intergenerational plants, which play a great role in the regulation of gene activity. Functional genomics showing the functions of genes, the functions of their protein products. The subject of the study of chronological genomics is the genome of different organisms, the divergence of which allows the understanding of the mechanisms of evolution of organisms, the unknown functions of genes. Genomics vinified on the cob of the 90s of the XX century at the same time from the project "Human Genome". The goal of this project was to determine the sequence of the ubiquit nucleotides in the human genome with an accuracy of up to 0.01%. Until the end of 1999, the future genome of dozens of species of bacteria, yeasts, round hrobak, drosophila, roslina arabidopsis will be revealed again. 2003 to the fate of deciphering the human genome. The human genome contains about 30 thousand proteins-coding genes. Only for 42% їх vіdoma їх molecular function. It turned out that less than 2% of all contagious diseases are associated with defects in the genes and chromosomes; 98% of the disease is due to disrupted regulation of the normal gene. Genes show their activity in synthesizing proteins, which are found in cells and organisms of various functions.
In the skin specific cells, at the same time, the singing dial of proteins is functioning. proteome. Proteomics- a science that develops the succession of proteins in clitins in different physiological states and in different periods of development, as well as the functions of these proteins. Mіzh genomics and proteomіkoyu є suttєva raznitsa - the genome is stable for this species, although the proteome is not only individual for different clitins of one organism, but also for one clitin in the fallow land in the country (podіl, calm, diferentiyuvannya toscho). Impersonal proteomes, dominating rich organisms, creating a great folding of their culture. For the time being, the exact number of proteins in the human body is unknown. For real estimates, there are hundreds of thousands; only a few thousand whites have already been seen, but less than a part of them have been reported. Identification and description of the whites is an overly complex technical process that requires a combination of biological and computer methods for analysis. However, the methods of revealing the products of the activity of genes - molecules and RNA and proteins, which are developed in the rest of the rocks, allow one to follow a rapid progress in this galus. Recently, methods have been created that allow one hour to detect hundreds of cells of proteins at the same time and to pair protein sets in different cells and tissues at normal levels for various pathologies. One of these methods is to win biological chips, which allow you to express in objects, which you speak, over a thousand different speeches: nucleic acids and proteins. The great possibilities of practical medicine are shown: a proteomic map, a report atlas of the whole complex of proteins, doctors who have chosen to take away the possibility of exercising the disease itself, but not the symptoms.
Genomics and proteomics operate on such majestic arrays of information that are necessary for the public bioinformatics- science, how to collect, sort, describe, analyze and process new information about genes and proteins. Vikoristovuyuchi mathematical methods and calculation technique, in the future will be genetic measures, modeling biochemical and other clinical processes. In 10-15 years, genomics and proteomics will reach such a level that we will be able to metabolome- A comprehensive scheme of interaction of all proteins in living cells. Experiments on clitins and organisms will be replaced by subsequent computer models. There will be a possibility of creating and stosuvannya іndivіdualnyh likarskih zasobіv, rozrobki іndivіdualnyh preventive visits. A particularly strong injection of new knowledge should be poured into biology development. We will be able to take into account the viability and at once to complete the details of the findings about individual cells, starting from the ovum and spermatozoa, and right up to the differentiation of the cells. Tse allow first, on a calculus basis, the interdependence of individual clitins at different stages of embryogenesis, which sacred world vchenih, yakі vvchayut biology development. New horizons are emerging in the solution of such problems as carcinogenesis and antiquity. The achievements of genomics, proteomics and bioinformatics should be added to the theory of evolution and systematics of organisms.
3 . Bilkova engineering
protein synthesis
The physical and chemical powers of natural proteins often do not satisfy the minds, in some numbers the proteins will vicariously become human. It is necessary to change the primary structure in order to ensure the formation of the protein with an earlier, lower, spacious structure and new physical and chemical authorities, which allow even in the minds of others to conquer the power of the natural protein functions. The design of the bilkiv is taken care of protein engineering. To remove the changed protein, vicorist methods combinatorial chemistry that zdіysnyuyut straightening mutagenesis- introduction of specific changes to DNA coding sequences, which lead to singing changes in amino acid sequences. For the effective design of the protein from the given power, it is necessary to know the regularity of the formation of the spacious structure of the protein, in order to lie down its physical and chemical power of that function, then it is necessary to know the primary structure of the protein, skin amino acid excess in plays on the power of that function of the protein. Unfortunately, the majority of proteins are not known to have a tretinous structure, which is always the same, as the very amino acid and the sequence of amino acids need to be changed in order to remove the proteins from the necessary power. Even now, with the help of computer analysis, one can predict the power of rich proteins, the sequence of their amino acid excesses. Similar analysis to simplify the procedure for the creation of required proteins. For the time being, in order to take into account the changes in proteins with the necessary powers, it is important to go the other way: to remove a sprat of mutant genes and know that protein product one of them, which may need authority.
For direct mutagenesis of vicory, there are different experimental approaches. Having eliminated the changes in the gene, it is possible to introduce the genetic construct into the prokaryotic or eukaryotic cells, which will increase the synthesis of the protein, which is encoded by the genetic construct.
The potential of protein engineering is similar to that of the attack.
By changing the ability of the binding of the speech, which is converted, - to the substrate - with the enzyme, it is possible to increase the catalytic efficiency of the enzymatic reaction.
By increasing the stability of the protein in a wide range of temperatures and the acidity of the middle, you can beat yoga in the minds, for which the protein is denatured, it wastes its activity.
Having created proteins that make them function in anhydrous retailers, you can create catalytic reactions in non-physiological minds.
4. By changing the catalytic center of the enzyme, it is possible to increase its specificity and change the number of unimportant side reactions
5. Raising the stability of the protein to the enzymes that it can be broken down, you can simplify the procedure for cleaning it.
b.Changing the protein in such a way, so that it can function instantly without a significant non-amino acid component (vitamin, a metal atom, etc.), you can win yoga in various uninterrupted technological processes.
7.Changing the structure of the regulatory cells of the enzyme, you can change the steps of the galvanization by the product of the enzymatic reaction for the type of negative serum linkage and thereby increase the excretion of the product.
8. You can create a hybrid protein that functions two and more proteins. 9. It is possible to create a hybrid protein, one of which will make it easier to use a hybrid protein from cells that are cultivated, otherwise it will improve yoga from sumish.
Knowing from the deakimthe reach of genetic engineering of proteins.
1. Replacing the sprat of amino acid residues in the lysozyme of bacteriophage T4 with cysteine removed the enzyme more disulfide bonds, which is why this enzyme retained its activity at a higher temperature.
2. Substitution of excess cysteine for excess serine in human r-interferon, which is synthesized by intestinal coli, outperformed the establishment of intermolecular complexes, while the antiviral activity of this drug was changed approximately 10 times.
3. Replacing excess threonine with excess proline in the enzyme tyrosyl-tRNA synthetase molecules increased the catalytic activity of this enzyme dozens of times: it became more efficient to add tyrosine to tRNA, which would transfer the qi amino acid ribosome during translation.
4. Subtilizini - rich in serine enzymes that break down proteins. The stench is secreted by rich bacteria that are widely vicorated by humans for biodegradation. The stench will mimic calcium atoms, which will promote stability. However, in the industrial processes there are chemical streaks that bind calcium, after which the subtilisins spend their activity. Having changed the gene, the scientists removed amino acids from the enzyme that take part in calcium binding, and they replaced one amino acid with another one in order to improve the stability of subtilisin. Changes in the enzyme appeared to be stable and functionally active in the minds close to industry.
5. Bula showed the possibility of the creation of an enzyme that functions according to the type of restrictases, which splits DNA in strictly designated areas. The scientists created a hybrid protein, one fragment of which recognized the same sequence of nucleotide residues in the DNA molecule, and the other split the DNA in this division.
6. Tissue plasminogen activator - an enzyme that is used in clinics to treat blood clots. It is a pity that the wines can be withdrawn from the blood circulation system and may have to be administered repeatedly, or at high doses, which can lead to side effects. Introducing three direct mutations in the gene of the enzyme, we removed the long-lived enzyme, which promoted sporulation to fibrin, which collapsed, and with the same fibrinolytic activity, like that of the enzyme.
7. By changing the change of one amino acid in the insulin molecule, the veins managed to get sick, if we suffer from diabetes, the change in the concentration of the hormone in the blood was close to physiological nogo, scho vinikaє after I receive it.
8. There are three classes of interferon, which may have antiviral and anti-cancer activity, but also show different specificity. It was tempting to create a hybrid interferon that could have the power of three types of interferons. We have created hybrid genes that include fragments of natural genes of interferons of decile types. Some of these genes, being introduced into bacterial cells, ensured the synthesis of hybrid interferons from a greater, lower in Batkiv molecules, anticancer activity.
9. Natural human growth hormone appears not only with the receptor of the first hormone, but also with the receptor of another hormone - prolactin. In order to get away from the unfortunate side effects In the process of healing the veins, it was possible to reduce the possibility of adding growth hormone to the prolactin receptor. The stench has reached this goal by replacing the active amino acids in the primary structure of growth hormone with the help of genetic engineering.
10. Anti-VIL-infection antivirals, the hybrid protein was taken away, one fragment of this protein was safely bound only to virus-infected lymphocytes, the other fragment prevented the penetration of the hybrid protein in the middle of the affected clitin, and one more fragment disrupting protein synthesis in the infected clitin led to death.
In this way, we have gone overboard in the fact that, by changing the specific cells of the protein molecule, we can give new powers to proteins, which we already know, and create unique enzymes.
Proteins are the main target for medicinal purposes. There are nearly 500 targets for children's faces across the country. Nearest rocks have a height of up to 10,000, which allows you to create new, efficient and safe faces. In the rest of the hour, fundamentally new approaches are being developed for the sake of medical research: as a target, not single proteins are seen, but their complexes, protein-protein interactions and protein folding.
Uploaded to the site
Types of mutual modality of non-allelic genes. The theory of F. Jacob and J. Mono about the regulation of i-RNA and protein synthesis. Dihybrid crossbreeding with non-powder dominance. Nealelny vzaєmodії genіv. The mechanism of regulation of the genetic code, the mechanism of induction-repression.
abstract, additions 29.01.2011
Differential expression of genes and their significance in the life of organisms. Peculiarities of regulation of gene activity in eukaryotes and their characteristics. Inducible and repres- sible operoni. Relatives and mechanisms of regulation of gene expression in prokaryotes.
lecture, contributions 10/31/2016
Mechanisms of functioning of living systems. Development of new biotechnological enzymes. Solution of Levinthal's phenomenon. Difficulty modeling whites. Methods for modeling the space structure of a protein. Exchange of porous modeling.
abstract, additions 28.03.2012
Provisions of the biological hypothesis of Jacob-Manot. The role of gene-regulators in the synthesis of proteins. Peculiarities of breaking the first stage of the process - transcription. Translation as an offensive step in biosynthesis. Fundamentals of enzymatic regulation of these processes.
presentation, added 01.11.2015
Physical, biological and chemical power of proteins. Synthesis and analysis of proteins. Designation of primary, secondary, tertiary and quarter structure of proteins. Denaturation, seeing that purification of proteins. Vykoristannya blіkіv v promyslovі and meditsinі.
abstract, additions 10.06.2015
Understanding, strategy, history and development of the reach of protein engineering. Potentiyni posibility її vikoristannya. The mechanism of site-specific mutagenesis. Possession of modified variants of natural proteins. Libraries of peptides and epitopes.
course work, donation 12/19/2015
Physical methods for follow-up of life. Deposition of biological activity of proteins in terms of their primary structure. Equal reaction of reamination of histidine and glyoxylic acid. Biologically active similar to the hormone adrenaline, their biosynthesis.
control of the robot, additions 10.07.2011
The study of the coding of the amino acid sequence of proteins and the description of the process of protein synthesis in ribosomes. genetic code and the synthesis of ribonucleic acid and Pobudov Lanziuga matrix RNA and protein synthesis. Broadcasting, throating and transportation of proteins.
abstract, additions 11.07.2015
The role of proteins in the signaling systems of clitin, in immune response and in the clitin cycle. See proteins in live clitins: enzymes, transport, grub, storage, fast-moving, rukhovi, structural, regulatory control. Domain structure of proteins.
presentation, added 10/18/2014
The concept of proteins is like high-molecular natural compounds (biopolymers) that are made up of excess amino acids, like a peptide bond. Functions and significance of proteins in the organism of a person, their transformation of that structure: primary, secondary, tertiary.
