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СПИСОК ЛИТЕРАТУРЫ
1 Ергожин Е.Е., Джиембаев Б.Ж., Барамысова Г.Т. Научное наследие академика М.И. Горяева. - Алматы.: Комплекс. 2004. - 540 с.
2 Джиембаев Б.Ж. а-Окси и а-аминофосфонаты шестичленных (N, O, S, Se) гетероциклов. - Алматы.: 2003.- 234 с.
3 Халилова С.Ф., Черманова Г.Б., Бутин Б.М. Селенаноны и их гидразоны / / Журн.общ. химии. - 1992. - Т 62. - №4. -С 851-854.
4 Бутин Б.М., Салимбаева А.Д. //Журн. общ.химии. - 1990. - Т 60. - №9. -С. 2171-2173.
5 Черманова Г.Б., Бутин Б.М. // Журн. общ.химии. - 1992. - Т 62. - №6.-С. 1314-1317.
6 Туканова С.К., Джиембаев Б.Ж., Халилова С.Ф., Бутин Б.М. //Журн. общ. химии. - 1992. - Т.62. - №6. -С. 2786-2787.
7 Ziriakus W., Hansel W., Haller R. //Arch. Pharm. und Ber. Dhsh. Pharmaz. Ger. 1971. Bd.304, №9. S.681-687.
8 Evers H., Christifens L., Renson M. // Tetrahedron Lett. - 1985. - V.26. - № 44. - P.5441-5442.
9 Жуманова Г.С., Джиембаев Б.Ж., Барамысова Г.Т., Фасхутдинов М.Ф. // Химический журнал Казахстана, 2006. - №2. -С 89-95.
10 Жуманова Г.С., Джиембаев Б.Ж., Барамысова Г.Т. //Вестник КазНУ. Сер. Хим. Алматы. - 2007. - №1(45). - С 135-137.
11 Абиюров Б.Д., Кулумбетова К.Ж., Джиембаев Б.Ж., Абдуллаев Н.Б., Казанбаева Л.С., Кияшев Д.К. /Сб. научн. трудов. Алма-Ата.: Наука. 1977. -С 139-146.
12 Кармерницкий А.В., Ахрем А.А.// Успехи химии. 1961. - Т30. - №.2. -С 145-183.
13 Barton D.H.R. // J. Chem. Soc. 1953. Р 1027-1040.
14 Barton D.H.R. //Suomen kem. 1959. V32. №2. A27-A33.
15 Унковский Б.В., Мохир И.А., Уринович Е.М. // Ж. общ. химии. 1963. - Т.33. - С. 1808-1816.
А.С.Кожамжарова, Л.С.Кожамжарова,* З.Б.Есимсеиитова**, Г.Т. Барамысова***
СЖАсфендияров атындагы К,азац улттыц медицина университетi *М.Х.Дулати атындагы Таразмеммекеттiкуниверситетi
**Эл-Фараби атындагы К,азащ улттьщ yumepcumemi ***Э.Б.Бектуров атындагы химия гылымдары институты
1С1ККЕ, ВИРУСЦА ^АРСЫ ЭРЕКЕТТ1 Ц¥РАМДЫ 2,6-ДИФЕНИЛСЕЛЕНАН-4-ОНА ЦИС-ИЗОМЕРЛ1 ФОСФОНИЛИРЛЕНУД1 ЗЕРТТЕУ
tywh: Диалкилфосфиттер нуклеофильд косылыстармен карбонильд топ 2,6-дифенилселенан-4-она цис-изомер стереоизомерл а-оксифосфонат экваториальды ориентациялы диалкоксифосфонатты топ изомерше ие болатын коспа тузетсндт корсетшген. Эпимерлердщ сандык катынасы аньщталып, стереоизомерл1 а-оксифосфонаттыц кещстштеп курылысы курастырылды.
ТYЙiндi свздер: ИК спектр, жука кабатты хроматография, 2,6-дифенилселенан-4-она, а-оксифосфонат, ¡сшке карсы, аритмияга карсы, вируска карсы.
A.S.Kozhamzharova, L.S.Kozhamzharova,* Z.B.Yesimseiltova,** G.T. Baramysova***
Asfendiyarov Kazakh National Medical University *M. Kh. Dulaty TarazState University ** al-Farabi Kazakh National University ***A.B.Bekturov Institute of Chemical Sciences
INVESTIGATION OF PHOSPHONYLATION OF CIS-ISOMER 2,6-DIPHENSIELELENAN-4-ON, INCLUDING ANTITUMOR, ANTI-VIRUSIVE
ACTION
Resume: It was shown that the mixture of stereoisomeric a-hydroxyphosphonates with predominance of the isomer with the equatorial orientation of the dialkoxyphosphonate group is formed during the nucleophilic addition of dialkylphosphites to the carbonyl group of the 2,6-diphenylselenane-4-one cis-isomer. The quantitative ratio of epimers is determined and the spatial structure of stereoisomeric a-hydroxyphosphonates is established.
Keywords: IR spectrum, thin layer chromatography, 2,6-diphenylselenane-4-one, а-hydroxyphosphonate, antitumor, antiarrhythmic, antiviral.
y^K 57.088/.012.6+615.071
A.S. Kozhamzharova, L.S. Kozhamzharova,* A.M. Karchalova, S.O. Ordabekov, Z.B. Yesimseiitova**
Asfendiyarov Kazakh National Medical University *M.Kh. Dulaty Taraz State University ** al-Farabi Kazakh National University
THE DIVERSITY AND CLASSIFICATION OF BIOMOLECULES AND MAIN IMPORTANCE OF BIOLOGICAL MACROMOLECULES FOR LIVING
ORGANISMS
In this article we regard about the diversity and classification of biomolecules and main importance of biological macromolecules for living organisms. This article has revealed a wealth of information about the biomolecules in living things. Processes such as glycolysis have been detailed by biochemical studies which have identified the roles of the biomolecules and their importance. Keywords: proteins, polysaccharides, phospholipids, lipids, macromolecules, carbohydrates, glycerol.
A biomolecule is a chemical compound found in living organisms. These include chemicals that are composed of mainly carbon, hydrogen, oxygen, nitrogen, sulfur and phosphorus. Biomolecules are the building blocks of life and perform important functions in living organisms. There are several types of biomolecules. Of most importance are the nucleosides and nucleotides that make up DNA and RNA, the molecules that are involved in heredity. There are also the lipids which function as
the building blocks of biological membranes and as energy providing molecules. The hormones serve in the regulation of metabolic processes and many other roles in organisms. The carbohydrates are also important in the provision of energy and as energy storage molecules. Amino acids and proteins function in many capacities in living organisms which include the synthesis of proteins, in the genetic code and as biomolecules that assist in other processes such as lipid transport. Vitamins are also necessary to the survival and health of organisms and
though not synthesized by organisms are important biomolecules [1-2].
The study of biomolecules is closely related to several fields such as molecular biology, biochemistry and genetics. Biochemistry is the study of the structure and function of biomolecules in organisms. This study has revealed a wealth of information about the biomolecules in living things. Processes such as glycolysis have been detailed by biochemical studies which have identified the roles of the biomolecules and their importance. It was previously thought that the molecules of life, biomolecules, could only be produced by living organisms. This view was however dispelled with the synthesis of urea. Today, a focus of biochemistry is the study of enzymes, biomolecules that are
made up of proteins. These biomolecules are essential to organisms as they speed up reactions that would normally take too long to sustain life. Other areas of interest in the study of biomolecules include the genetic code and cell membrane transport.
Amino Acids Are the Building Blocks of Proteins
Although proteins are complex and versatile molecules, they are all polymers of only 20 amino acids, in a specific order. Many scientists believe amino acids were among the first molecules formed in the early earth. It seems highly likely that the oceans that existed early in the history of the earth contained a wide variety of amino acids.
Figure 1 - Amino Acid Structure [2]
An amino acid is a molecule containing an amino group (— NH2), a carboxyl group (—COOH), and a hydrogen atom, all bonded to a central carbon atom: Each amino acid has unique chemical properties determined by the nature of the side group (indicated by R) covalently bonded to the central carbon atom.
For example, when the side group is —CH2OH, the amino acid (serine) is polar, but when the side group is —CH3, the amino acid (alanine) is nonpolar. The 20 common amino acids are grouped into five chemical classes, based on their side groups:
Figure 2 - Structural features of amino acids (shown in their fully protonated form)
1. Nonpolar amino acids, such as leucine, often have R groups that contain —CH2 or —CH3.
2. Polar uncharged amino acids, such as threonine, have R groups that contain oxygen (or only —H).
3. Ionizable amino acids, such as glutamic acid, have R groups that contain acids or bases.
4. Aromatic amino acids, such as phenylalanine, have R groups that contain an organic (carbon) ring with alternating single and double bonds.
5. Special-function amino acids have unique individual properties; methionine often is the first amino acid in a chain of amino acids, proline causes kinks in chains, and cysteine links chains together. Each amino acid affects the shape of a protein differently depending on the chemical nature of its side group.
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Portions of a protein chain with numerous nonpolar amino acids, for example, tend to fold into the interior of the protein by
Amino acid
hydrophobic exclusion [5]. Amino acid
H ® 1
H- N 1 -c-1 C—'QH 1 -
1 H 1 0
H ® 1
H)—N 1 — c-1 C-OH 1
1 H 1 0
H,0
Polypeptide chain
H ® 1 H 1 ® 1
H— N 1 -c-1 c-1 N- - c-1 C—OH II
1 H 1 0 1 H II o
The peptide bond. A peptide bond forms when the —NH2 end of one amino acid joins to the —COOH end of another. Because of the partial double-bond nature of peptide bonds, the resulting peptide chain cannot rotate freely around these bonds [6]. Proteins Are Polymers of Amino Acids
In addition to its R group, each amino acid, when ionized, has a positive amino (NH3 +) group at one end and a negative carboxyl (COO-) group at the other end. The amino and carboxyl groups on a pair of amino acids can undergo a condensation reaction, losing a molecule of water and forming a covalent bond. A covalent bond that links two amino acids is called a peptide bond. The two amino acids linked by such a bond are not free to rotate around the N—C linkage because the peptide bond has a partial double-bond character, unlike the N—C and C—C bonds to the central carbon of the amino acid. The stiffness of the peptide bond is one factor that makes it possible for chains of amino acids to form coils and other regular shapes. A protein is
Figure 3.
composed of one or more long chains, or polypeptides, composed of amino acids linked by peptide bonds. It was not until the pioneering work of Frederick Sanger in the early 1950s that it became clear that each kind of protein had a specific amino acid sequence. Sanger succeeded in determining the amino acid sequence of insulin and in so doing demonstrated clearly that this protein had a defined sequence, the same for all insulin molecules in the solution. Although many different amino acids occur in nature, only 20 commonly occur in proteins. Figure 3.6 illustrates these 20 "common" amino acids and their side groups.
A Protein's Function Depends on the Shape of the Molecule
The shape of a protein is very important because it determines the protein's function. If we picture a polypeptide as a long strand similar to a reed, a protein might be the basket woven from it.
Figure 4 - The variety of proteins within a cell
Overview of Protein Structure
Proteins consist of long amino acid chains folded into complex shapes. What do we know about the shape of these proteins? One way to study the shape of something as small as a protein is to look at it with very short wavelength energy—with X rays. X-ray diffraction is a painstaking procedure that allows the investigator to build up a three dimensional picture of the position of each atom.
The first protein to be analyzed in this way was myoglobin, soon followed by the related protein hemoglobin. As more and more proteins were added to the list, a general principle became evident: in every protein studied, essentially all the internal amino acids are nonpolar ones, amino acids such as leucine,
valine, and phenylalanine. Water's tendency to hydrophobically exclude nonpolar molecules
literally shoves the nonpolar portions of the amino acid chain into the protein's interior. This positions the nonpolar amino acids in close contact with one another, leaving little empty space inside. Polar and charged amino acids are restricted to the surface of the protein except for the few that play key functional roles [6].
Levels of Protein Structure
The structure of proteins is traditionally discussed in terms of four levels of structure, as primary, secondary, tertiary, and quaternary (figure 3.4). Because of progress in our knowledge of protein structure, two additional levels of structure are increasingly distinguished by molecular biologists: motifs and
domains. Because these latter two elements play important roles in coming chapters, we introduce them here. Primary Structure.
The specific amino acid sequence of a protein is its primary structure. This sequence is determined by the nucleotide sequence of the gene that encodes the protein. Because the R groups that distinguish the various amino acids play no role in the peptide backbone of proteins, a protein can consist of any sequence of amino acids. Thus, a protein containing 100 amino acids could form any of 20100 different amino acid sequences (that's the same as 10130, or 1 followed by 130 zeros—more than the number of atoms known in the universe). This is an important property of proteins because it permits such great diversity.
Secondary Structure. The amino acid side groups are not the only portions of proteins that form hydrogen bonds. The —COOH and —NH2 groups of the main chain also form quite good hydrogen bonds—so good that their interactions with water might be expected to offset the tendency of nonpolar sidegroups to be forced into the protein interior. Inspection of the protein structures determined by X-ray diffraction reveals why they don't—the polar groups of the main chain form hydrogen bonds with each other! Two patterns of H bonding occur. In one, hydrogen bonds form along a single chain, linking one amino acid to another farther down the chain. This tends to pull the chain into a coil called an alpha (a) helix. In the other pattern, hydrogen bonds occur across two chains, linking the amino acids in one chain to those in the other. Often, many parallel chains are linked, forming a pleated, sheetlike structure called a p-pleated sheet. The folding of the amino acid chain by hydrogen bonding into these characteristic
coils and pleats is called a protein's secondary structure [5]. Tertiary Structure
The final folded shape of a globular protein, which positions the various motifs and folds nonpolar side groups into the interior, is called a protein's tertiary structure. A protein is driven into its tertiary structure by hydrophobic interactions with water. The final folding of a protein is determined by its primary structure— by the chemical nature of its side groups. Many proteins can be fully unfolded ("denatured") and will spontaneously refold back into their characteristic shape. The stability of a protein, once it has folded into its 3-D shape, is strongly influenced by how well its interior fits together. When two nonpolar chains in the interior are in very close proximity, they experience a form of molecular attraction called van der Waal's forces. Individually quite weak, these forces can add up to a strong attraction when many of them come into play, like the combined strength of hundreds of hooks and loops on a strip of Velcro. They are effective forces only over short distances, however; there are no "holes" or cavities in the interior of proteins. That is why there are so many different nonpolar amino acids (alanine, valine, leucine, isoleucine). Each has a different- sized R group, allowing very precise fitting of nonpolar chains within the protein interior. Now you can understand why a mutation that converts one nonpolar amino acid within the protein interior (alanine) into another (leucine) very often disrupts the protein's stability; leucine is a lot bigger than alanine and disrupts the precise way the chains fit together within the protein interior. A change in even a single amino acid can have profound effects on protein shape and can result in loss or altered function of the protein. Simple Carbohydrates Carbohydrates function as energy-storage molecules as well as structural elements. Some are small, simple
molecules, while others form long polymers. Sugars Are Simple Carbohydrates The carbohydrates are a loosely defined group of molecules that contain carbon, hydrogen, and oxygen in the molar ratio 1:2:1. Their empirical formula (which lists the atoms in the molecule with subscripts to indicate how many there are of each) is (CH2O)n, where n is the number of carbon atoms. Because they contain many carbon-hydrogen (C—H) bonds, which release energy when they are broken, carbohydrates are well suited for energy storage. Monosaccharides. The simplest of the carbohydrates are the simple sugars, or monosaccharides (Greek mono, "single" + Latin saccharum, "sugar"). Simple sugars may contain as few as three carbon atoms, but those that play the central role in energy storage have six (figure 6). The empirical formula of six-carbon sugars is: C6H12O6, or (CH2O)6 Six-carbon sugars can exist in a straight-chain form, but in an aqueous environment they almost always form rings. The most important of these for energy storage is glucose (figure 6), a six-carbon sugar which has seven energystoring C—H bonds [4]. Reaction results, discussions and conclusion upon research Qualitative identification of amino acids
Amino acids are building blocks of all proteins, and are linked in series by peptide bond (-CONH-) to form the primary structure of a protein. Amino acids possess an amine group, a carboxylic acid group and a varying side chain that differs between different amino acids.
There are 20 naturally occurring amino acids, which vary from one another with respect to their side chains. Their melting points are extremely high (usually exceeding 200°C), and at their pH, they exist as zwitterions, rather than as unionized molecules. Amino acids respond to all typical chemical reactions associated with compounds that contain carboxylic acid and amino groups, usually under conditions where the zwitter ions form is present in only small quantities. All amino acids (except glycine) exhibit optical activity due to the presence of an asymmetric a - Carbon atom. Amino acids with an L - configuration are present in all naturally occurring proteins, whereas those with D - forms are found in antibiotics and in bacterial cell walls. Certain functional groups in amino acids and proteins can react to produce characteristically coloured products. The colour intensity of the product formed by a particular group varies among proteins in proportion to the number of reacting functional or free groups present and their accessibility to the reagent. Now we will discuss various colour-producing reagents (dyes) to qualitatively detect the presence of certain functional groups in amino acids and proteins. There are six tests for the detection of functional groups in amino acids and proteins. The six tests are: (1) Ninhydrin Test (2) Biuret Test (3) Xanthoproteic Test (4) Millon's Test (5) Hopkins-Cole Test and
(6) Nitroprusside Test.
Ninhydrin Test
Ninhydrin (1,2,3-Indantrione monohydrate, or triketohydrindene hydrate) is often used to detect CC-amino acids and also free amino and carboxylic acid groups on proteins and peptides. When about 0.5 mL of a 0.1% solution of ninhydrin is boiled for one or two minutes with a few mL of dilute amino acid or protein solution, a blue color develops. A ninhydrin solution in ethanol or other volatile solvents is often used as a developer for amino acids in paper chromatography or thin layer chromatography. Ninhydrin spray is also used on crime scenes to visualize fingerprints, which contain trace amounts of amino acids.
Figure 5 - Chemical structure of
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Ninhydrin degrades amino acids into aldehydes, ammonia, and CO2 through a series of reactions; the net result is ninhydrin in a partially reduced form hydrindantin: Ninhydrin then condenses
with ammonia and hydrindantin to produce an intensely blue or purple pigment, sometimes called Ruhemann's purple:
0
ninhydrin
NH,,
partially reduced form
Figure 6 - The production
The color varies slightly from acid to acid, probably because unreacted acids complex with the pigment. Proline and hydroxyproline give a yellow color. Since all that is required for color development is ammonia and partially reduced ninhydrin, the ammonium salts of weak and strong acids, as well as certain amines, can give a false positive result to the ninhydrin test. Reagents:
0,1 % solution of amino acids
1,0% solution of protein (egg white protein)
0,1% solution of ninhydrin
Procedure
Prepare test tubes:
Test tube: 0,2 ml of 0,1% solution of amino acids Test tube: 0,2 ml of 1,0 % solution of protein' Test tube: 0,2 ml of water (control sample)
To each of the test tubes, add 0,1 ml of 0,1% ninhydrin reagent and heat the test tubes in a boiling water bath for about 1-2 minutes. The ninhydrin test is a test for amino acids and proteins with a free -NH2 group. When such a -NH2 group reacts with ninhydrin, a blue complex is formed.
Conclusion Cells are largely composed of compounds that contain carbon. The study of how carbon atoms interact with other atoms in molecular compounds forms the basis of the field of organic chemistry and plays a large role in understanding the
of Ruhemann's purple [5].
basic functions of cells. Because carbon atoms can form stable bonds with four other atoms, they are uniquely suited for the construction of complex molecules. These complex molecules are typically made up of chains and rings that contain hydrogen, oxygen, and nitrogen atoms, as well as carbon atoms. These molecules may consist of anywhere from 10 to millions of atoms linked together in specific arrays. Most, but not all, of the carbon-containing molecules in cells are built up from members of one of four different families of small organic molecules: sugars, amino acids, nucleotides, and fatty acids. Each of these families contains a group of molecules that resemble one another in both structure and function. In addition to other important functions, these molecules are used to build large macromolecules. Biological Macromolecules Some organic molecules in organisms are small and simple, containing only one or a few functional groups. Others are large complex assemblies called macromolecules. In many cases, these macromolecules are polymers, molecules built by linking together a large number of small, similar chemical subunits, like railroad cars coupled to form a train. For example, complex carbohydrates like starch are polymers of simple ring-shaped sugars, proteins are polymers of amino acids, and nucleic acids (DNA and RNA) are polymers of nucleotides.
REFERENCES
1. Biochemistry and Molecular Biology, 2nd ed. New Delhi.: Oxford University Press, 2003. - P 100.
2. Biochemistry Terminology, Delhi : Lakshay Publicaton, 2003. P 50.
3. Biochemistry, 3rd ed. India : Pearson Education Asia Pte. Ltd., 2003. P 78.
4. Chemistry: foundations and applications by J.J. Lagowski ISBN: 002865721 Publication Date: 2004. P 100.
5. D. T. Plummer, An Introduction to Practical Biochemistry, Tata McGraw Hill, New Delhi.: 2004. P 86.
6. E. E. Conn and P. K. Stumpf, Outlines of Biochemistry, John Wiley & Sons, New York.: 2004. P 50.
7. Encyclopedia of Biological Chemistry by William J. Lennarz Second edition. ISBN: 9780123786319 Publication Date: 2013. P 98.
А.СДожамжарова, Л.СДожамжарова, * Карчалова А.М, С.О.Ордабеков, З.Б.Есимсеиитова**
СЖАсфендияров атындагы Казац улттыц медицина университетi *М.Х.Дулати атындагы Таразмемлекеmmiкуниверсиmеmi **Эл-Фараби атындагы Казац улттыцуниверситетi
Т1Р1 АFЗАЛАР УШ1Н БИОЛОГИЯЛЬЩ МАКРОМОЛЕКУЛАЛАРДЬЩ НЕГ1ЗД1Л1П ЖЭНЕ БИОМОЛЕКУЛАЛАРДЫН,
Ж1КТЕЛ1НУ1МЕН ТУРЛ1Л1П
tywh: Макалада Tipi агзалар ушш биологиялы; макромолекулалардыц непздШп жэне биомолекулалардыц жштелш^мен турлШп карастырылган. Tipi агзалардагы биомолекулалы; акпараттар нактылы суреттелш ашы; турде сипатталган. Процестер, мысалы гликолиз сия;ты, биохимиялы; зерттеулерде нактылай сипатталып, биомолекулалардыц непзп pолi жэне олардыц мацыздылыгы
tywh4ï сездер: акуыздар, полисахаридтер, фосфолипидтер, липидтер, макромолекулалар, квмipсугектеp, глицерин.
А.С.Кожамжарова, Л.С.Кожамжарова,* Карчалова А.М, С.О.Ордабеков, З.Б.Есимсеиитова**
Казахский Национальный медицинский университет имени С.Д.Асфендиярова *Таразский Государственный университет имени М.Х.Дулати **Казахский Национальный университет имени аль-Фараби
РАЗНООБРАЗИЕ, КЛАССИФИКАЦИЯ БИОМОЛЕКУЛ И ГЛАВНОЕ ЗНАЧЕНИЕ БИОЛОГИЧЕСКИХ МАКРОМОЛЕКУЛ ДЛЯ ЖИВЫХ
ОРГАНИЗМОВ
Резюме: В статье мы рассматриваем разнообразие и классификацию биомолекул и основное значение биологических макромолекул для живых организмов. Раскрыта обширная информация о биомолекулах в живых существах. Процессы, такие как гликолиз, были подробно описаны в биохимических исследованиях, в которых определены роли биомолекул и их важность. Ключевые слова: белки, полисахариды, фосфолипиды, липиды, макромолекулы, углеводы, глицерин.
