BIOLOGICAL MOLECULES E/ souwiteabiet + Introduce biochemistry and describe the approximate chemical composition of protoplasm. + Distinguish carbohydrates, proteins, lipids and nucleic acids as the four fundamental kinds of biological molecules. ‘+ Describe and draw sketches of the dehydration-synthesis and hydrolysis reactions for the making and breaking of macromolecule polymers. + Explain the following properties of water that make it the cradle of life high potarity, hydrogen bonding, high specific heat high heat of vaporization cohesion, hydrophobic exclusion ionization lower density of ice * Define carbohydrates and classify them. ‘+ Distinguish the properties and roles of monosaccharides, write their empirical formula and classify them. ‘+ Compare the isomers and stereoisomers of glucose. ‘+ Distinguish the properties and roles of disaccharides and describe glycosidic bond in the transport disaccharides. + Distinguish the properties and roles of polysaccharides and relate them with the molecular structures of starch, glycogen, cellulose and chitin. ‘+ Justify that the laboratory-manufactured sweeteners are “left-handed” sugars and cannot be metabolized by the “right-handed” enzymes. + Define proteins and amino acids and draw the structural formula of amino acid ‘+ Outline the synthesis and breakage of peptide linkages. + Justify the significance of the sequence of amino acids through the example of sickle cell hemoglobin. * Classify proteins as globular and fibrous proteins. ‘+ List examples and the roles of structural and functional proteins. + Define lipids and describe the properties and roles of aoylglycerols, phospholipids, terpenes and waxes. + Ilustrate the molecular structure (making and breaking) of an acylglycerol, a phospholipid and a terpene.2 Biological Molecules ‘+ Evaluate steroids and prostaglandins as important groups of lipids and describe their roles in living organisms, * Define nucleic acids and nucleotides. ‘© Describe the molecular level structure of nucleotide, ‘= Distinguish among the nitrogenous bases found in the nucleotides of nucleic acids. * Outline the examples of a mononucleotide (ATP) and a dinucleotide (NAD). ‘© Explain the double helical structure of DNA as proposed by Watson and Crick. * Define gene is a sequence of nucleotides as part of DNA, which codes for the formation of a polypeptide. + Explain the general structure of RNA. * Distinguish in term of structures and roles, the three types of RNA. = Define conjugated molecules and describe the roles of common conjugated molecules i.e. alycolipids, glycoproteins, lipoproteins and nucleoproteins. You have got a very brief introduction about biological molecules in IX-X biology course. This chapter caters the detailed study of carbohydrates, proteins, lipids and nucleic acid as well as the importance of water and the role of conjugated molecules. 2.1 BIOLOGICAL MOLECULES IN PROTOPLASM Biological molecules are different chemical compounds of living beings. Biochemistry is the branch of biology that deals with such molecules. It also deals with various chemical reactions (metabolism) of living beings. 2.1.1 Chemical Composition of Protoplasm Approximately 25 elements 70% out of 92 naturally occurring fix majo biclanat that elements of earth are found in living constitute 99% of human body beings. These are called soy, Onygen 65% bioelements. However, human body ieee on is composed of only 16 of these 40% Nitrogen 3% bioelements. These elements can be py, Cacum 2% Phosphorus 1% classified on the basis of their proportions in organisms. The six 20% commonest —bioelements _ that constitute 99% of protoplasm are called major bioelements. Minor 0% - bioelements are those that are found Orygen Carbon _Hysrogen Mtogen Calcium Phosphorus as less than 1% whereas those that Minor elements include: potassium (0.35%), sulphur (0.25%), are found as less than 0.01% of the | chiorine (0.15%), sodium (0.15%) and magnesium (0.05%) protoplasm are called trace | Trace elements include iron, copper, manganese, zinc 10% elements. The proportions of these Fig, 2.1: Proportions of various bioelements in human bodygz 2 Biological Molecules elements are given in the fig: 2.1. Some trace elements such as iron are needed by all forms of life. Others are required only by certain species. The bioelements are combined with each other and can form thousands of different biomolecules which may be inorganic (water and minerals) and organic (carbohydrates, lipids, proteins and nucleic acids). The proportions of these biomolecules are given in the table. Table 2.1: Proportions of various biomolecules in bacterial and mammalian cells | so ee Water 70% 70% Protea 18% 78% Carbohydrates 3% 4% Unis 2% a ONA 1% 025% RNA % 1% (fier Sane ricloues(orzyreshonmonos etal) 2% 2% Inorganic fons (Na’, K", Ca", Mg++, CI, S047) 1% 1% The four fundamental kinds of biological molecules are carbohydrates, proteins, lipids and nucleic acids. Carbohydrates are present in the cytoplasm of the cells and provide fuel for the metabolic activities of the cell. Proteins are present in the membranes, ribosomes, cytoskeleton and enzymes of the cell. Lipids are present in the membranes and cytoplasm of the cell. Lipids provide a reserved energy source, shape, protect and insulate the cells. The nucleic acid DNA is present in the chromosome. It controls the cell activity. The nucleic acid RNA is present in the nucleoplasm and cytoplasm. It takes genetic information from DNA and play role in protein synthesis. 2.1.2 Condensation and Hydrolysis A macromolecule is high molecular weight compound which is made from many repeating units. Molecules built like this are also known as polymers. The individual units of polymers are micromolecules which are also known as monomers. The interconversions of these molecules are carried out by condensation and hydrolysis. During condensation, when two monomers join, a hydroxyl (-OH) group is removed from one monomer and a hydrogen (-H) is removed from the other to make water and as a result a bond is synthesized between the monomers. The product of such reaction is called a ae oe = acd a Fig: 2.2: Monomer and polymer O.,. Saat ee eecccee,, Fig. 2.3: Condensation and Hydrolysis@ 2 Biological Molecules dimer. If the same reaction is repeated several times the resulting molecule will be a polymer. ; a Condensation is also called dehydration synthesis Science Titbits . because water is removed (dehydration) and bond odie cori ee vo cel elu in hydrolysis with making a solution, in which is made (synthesis). Condensation does not take | the role of water is to act as a solvent, rather place unless the proper enzyme is present and the | than taking part in a chemical reaction. Also monomers are in an activated energy- rich form. do not assume that this breakdown releases , energy, which is usually produced when the The hydrolysis is essentially the reverse of | simpier substances are oxidized in condensation i.e., the breakdown of a polymer into | respiration. Hydration is yet another its monomers by the addition of water. During | completely different process, involving the hydrolysis, an (-OH) group from water is attached | addition of water, but not breaking of bonds to one monomer and (-H) is attached to the other monomer. Actually all digestion reactions are examples of hydrolysis, which are controlled by enzymes such as carbohydrases, proteases, lipases, nucleases. 2.2 IMPORTANCE OF WATER Water is one of the main constituents on earth. More than two thirds of the earth is covered by water. Approximately 70 percent of the any organism is formed of water. Water is the most abundant component in any organism, the lowest is 20% in seeds and bones and highest is 85-90% in brain cells. Jellyfish has exceptionally large amount of water i.e., 99% (hence the body shows transparency). Critical Thinking “ When hydrogen gas 2.2.1. Properties of water combines with oxygen gas i to form water, is the The properties of water that make it the cradle of life are: ee 1. High polarity oxidized? The bonds which are formed by the mutual sharing of electrons between two atoms are called covalent bonds. Normally the sharing of electrons between two atoms is fairly equal and the covalent bond is nonpolar. In the case of water, however the sharing of electrons between oxygen and hydrogen is not completely equal so the covalent bond is polar. A polar covalent bond is a chemical bond in which shared electrons are pulled closer to the more electronegative atom, making it partially negative and the other atom partially positive. Thus, in HO, the O atom actually has a slight negative charge and each H atom has a slight positive charge, even though H20 as a whole is neutral. Because of its polar covalent bonds, water is a polar molecule i.e., it has a slightly negative pole and two slightly positive ones. Fig: 2.4: Polarity of water molecule This is polarity of water molecules that makes it an excellent or universal solvent for polar substances. lonic compound or electrolytes can be easily dissolved in water, non-polar substances having charged groups in their molecules can also be dissolved in water. Such"2 Biological Molecules compounds when dissolved in water, disassociates into positive and negative ions and are in more favourable state to react with other molecules and ions. This is the reason why all chemical reactions in living beings occur in aqueous medium. 2. Hydrogen bonding The polarity of water molecules makes them interact with each other. The charged regions on each molecule are attracted to oppositely charged regions on neighbouring molecules, forming weak bonds. Since the positively charged region in this special type of bond is always an H atom, the bond is called a hydrogen bond. This bond is often represented by a dotted line because a hydrogen bond is easily broken Hydrogen bond Because of hydrogen bonding, water is a liquid at temperatures suitable for life. The high cohesion and adhesion force of water is due to the presence of hydrogen Fig: 2.5 Hydrogen bonds between bonds in water, which in turns makes water as transport water molecules medium. 3. Cohesion and adhesion Cohesion is the attraction among the water molecules which enables the water molecules to stick together. Water flows freely due to cohesion. Water molecules also have attraction to polar surfaces. This attraction is called adhesion. Both cohesion and adhesion are due to hydrogen bonds among water molecules. These properties of water enable it to circulate in living bodies and to act as transport medium. 4. High specific heat capacity Heat capacity can be defined as the amount of heat required for minimum increase in temperature of a substance. The specific heat capacity of water can be represented as number of calories required to raise the temperature of 1g of water up to 1°C i.e., 1 Calorie (4.18 Joules). Water has relatively a very high heat capacity than any other substance due to its hydrogen bonding, because much of the heat absorbed by water is utilized in the breakdown of hydrogen bonding therefore it does not manifest itself to raise the temperature of water. Hence, very large amount of heat can increase very little in temperature in water. Due to its high heat capacity water works as temperature stabilizer or regulator for organisms in the hot environment and hence protects the living material against sudden thermal changes. 5. High heat of vapourization Heat of vapourization is the amount of heat required to convert a unit mass of a liquid into gaseous form. Heat of vapourization of water is represented as number of calories absorbed per gram vapourized. Water has high heat of vapourization i.e., 574 calories per gram. The high heat of vapourization means that a large amount of heat can be lost with minimal loss of water from the body. This is high heat of vapourization of water that gives animals an efficient way to release excess body heat in a hot environment. When an animalo = 2 Biological Molecules a5) oe sweats, body heat is used to vapourize the sweat thus cooling the animal. Due to this property of water, evaporation of only 2 ml out of one litter of water lowers the temperature of the remaining 998 ml water by 1°C. 6. Hydrophobic exclusion Hydrophobic exclusion can be defined as reduction of the — contact. «area between water and hydrophobic substances which are placed in water. For example, if you place few drops of oil on the surface of a water solution, the oil drops will tend to join into a single drop. Biologically, hydrophobic exclusion plays key roles in maintaining the integrity of lipid bilayer membranes. 7. lonization lonization The dissociation of a molecule into ions HWH — Hu baa Ul is called ionization. When water molecule Fig: 2.6: Hydrophobic exclusion ionizes, it releases an equal number of positive Water molecule Hydroxyl ion Hydrogen ion hydrogen and negative hydroxyl ions. (HO) [0H] WW) This reaction is reversible but Seed ec reny equilibrium is maintained at 25°C. The H* and OH‘ ions affect and take part in many of the reactions that occur in cells, e.g., it helps to maintain or change the pH of the medium 8. Lower density of ice Ice floats on water. This is because ice is less dense than water. The reason is that ice has a giant structure and show maximum number of hydrogen bonding among water molecules; hence, they are arranged like a lattice. In freezing weather, ice forms on the surface of ponds and lakes forming an insulating layer above the water below. This provides a living environment for some organisms until the ice melts. Fig: 2.8: Lattice kes arrangement Organisms can also live under the ice. ‘of water molecules in ice Skills: Analyzing, Interpreting and Communication * Draw model diagrams to describe the hydrogen bonding, 2.3 CARBOHYDRATES Carbohydrates are the compounds of carbon, hydrogen and oxygen. Literally word carbohydrate means “hydrates of carbon" i.e., a carbon associated with water. Chemically carbohydrates are:gz 2 Biological Molecules “Organic compounds that are polyhydroxy H aldehydes or polyhydroxy ketones, or change to such H. substances on simple chemical transformations, as hydrolysis, oxidation, or reduction.” 2.3.1 Classification of Carbohydrates Carbohydrates are commonly known as sugars or saccharides because more familiar '——C——OH Pe aon carbohydrates have sweet taste. Classification of | | carbohydrates is based upon number of saccharide H H units. Carbohydrates are generally classified into Polyhydroxy Polyhydrony three group i.e., monosaccharides, oligosaccharides aldehyde ketone and polysaccharides. Fig: 2.9: Chemical nature of carbohydrates Table: 2.2: Comparison of characteristics of carbohydrates They consist of single saccharide unit They are composed of 2 to 10 saccharide units. They are composed of more than 10 saccharide units. They are simplest carbohydrates; therefore, they cannot be further hydrolyzed They have less complex structure, so upon hydrolysis they yield at least 2 and maximum 10 monosaccharides. They have highly complex structure, so upon hydrolysis they yield at least 11 monosaccharides. They are highly soluble in water. ‘They are less soluble in water. They are generally insoluble in water. They are sweetest among all They are less sweet in taste. They are tasteless. carbohydrates, 2.3.2 Monosaccharides Monosaccharides are true carbohydrates which are either polyhydroxy aldehydes or polyhydroxy ketones. The range of number of carbons in monosaccharides is 3 to 7. All the carbon atoms in a monosaccharide except one, have a hydroxyl group (-OH) while the remaining carbon atom is either the part of aldehyde or ketone. The general formula for the representation of monosaccharides is C,H2,n, where, n is the number of carbon atoms in monosaccharides Classification of monosaccharides Classification of monosaccharides is based upon functional group and number of carbon atoms. On the basis of functional group, the monosaccharides containing aldehyde are called aldoses while those containing ketone are called ketoses. On the other hand monosaccharides are classified into five groups based upon number of carbon atoms i.e., trioses (3C), tetroses (4C), pentoses (5C), hexoses (6C) and heptoses (7C).© 2 iotogical Molecules Table: 2.3: Examples and functions of monosaccharides Trioses C3He03 Glyceraldehyde | Dihydroxy Intermediates in photosynthesis and cellular (acy acetone respiration Tetroses | CyHsOx Erythrose Erythrulose Intermediates in bacterial photosynthesis. (4c) Pentoses [C:HiOs | Ribose, Ribulose Ribose and deoxyribose are components of (6c) Deoxyribose RNA and DNA respectively (Cst4ie0s) Ribbulose is an intermediates in photosynthesis, Hexoses | CeH205 Glucose, Fructose Glucose is respiratory fuel (initial substrate) (6c) Galactose Fructose is an intermediate in respiration. Galactose is the component of milk sugar. Heptoses | G;H,.0; | Glucoheptose | Sedoheptulose | inlermediates in photosynthesis. (rey Chemical structures of monosaccharides IcHo Monosaccharides are usually found in open bon O# chain structure in crystalline form but when they are 3 4 dissolved in water most of them (pentoses and HOC-OH eos hexoses) are converted into ring chain structure. H=C—OH ‘OH OH 3 Let us understand it by taking ribose Sh OH ing stuctre by (CsH;o0s) as an example. It can exist in open chain Rose structure in dried form but it exists in ring structure in aqueous medium. When it is dissolved in water, the oxygen atom from aldehyde group reacts with ‘second last carbon i.e., C4 in case of ribose. In this way oxygen atom forms a link between C1 and C4 while the OH group of C4 is shifted to C1. After this (open chain structure) Fig: 2.10: Conversion of open chain into ring chain «@H,0H «@H,0H modification ring structure of ribose gy y 16 is formed. / / # \ c or Each pentose or hexose Ko V8 oe #0 ‘ #0 ( molecule in ring structure exists in HCs—OH either a or B form depending upon on nie OH: I -Giucose P-Giucose H—c.—o# the position of -H and -OH group on I Cl. If -OH group is found Fig: 242: aand isomers of glucose 4 : Fig: 2.11: Glucose downward on C-1 then itis called a sugar and if -OH is present upward ‘open chain structure on C-1 then it is known as B sugar as shown in the fig: 2.12. Stereoisomerism in Glucose Stereoisomers are molecules that have the same molecular formula and differ only in how atoms are arranged in 3D space. Enantiomers is a type of stereoisomers in which molecules© 2 siotogica Molecules are nonsuperimposable mirror-images. This means that the molecules are mirror image but they cannot be placed on top of one another to give the same molecule. An example of enantiomer is D and L glucose. D sugars are right handed ea oom 4 “My and L sugars are left handed molecules. ot \ oH if ‘nfo NE i Laboratory Manufactured (Artificial) Sweeteners iy i Laboratory manufactured sugars are L sugars. On the —_—_L-gucose ech other hand the naturally occurring sugars in bodies are D —_iinitwm tevin sugars. Proteins and cell receptors are designed to react Fig: 2.13: An example of enantiomers only with D sugars. For example the enzymes in your stomach can digest only right-handed sugars. Likewise left-handed sugars cannot be metabolized by right-handed enzymes. Just as the glove fits only on the proper hand, a right- handed enzyme cannot fit on or react with a left-handed substrate. The substrate must fit on the proper active site of the enzyme. So for the left handed substrate (artificial sweetener) the enzyme must be left-handed. 2.3.3 Oligosaccharides This group consists of derivatives of monosaccharides. Those carbohydrates which upon hydrolysis yield 2 to 10 saccharide units are called oligosaccharides. On the basis of number of saccharide units, the oligosaccharides are classified into disaccharides, trisaccharides, tetrasaccharides and so on. The most common among these are disaccharides. Disaccharides Two monosaccharides combine to form a disaccharide. It is a kind of oligosaccharides. Disaccharides are less sweet in taste and less soluble in water. These can be hydrolyzed to give monosaccharides. Examples are: maltose, lactose, sucrose. The general formula of disaccharide is: C12 Hz2 O1;. Some common disaccharides are as follows: Sucrose: It is commonly known as cane sugar. It is widely used as sweetener at homes for making sweet dishes. In plants sucrose is also called transport disaccharide as prepared food in plants is transported in the form of sucrose. It is very soluble and can therefore be moved efficiently in high concentration in plants. It is also relatively unreactive chemically. The sucrose is formed by the condensation of glucose and fructose. In this reaction, the -OH group at C-1 of glucose reacts with the -OH group at C-2 of fructose, liberating a water molecule forming a-1,2-glycosidic linkage. HOSH, Hosh, GH.OH HOH a-Glucose - Fructose Sucrose Water a -4.2-6iyeasc linkage Fig: 2.14: Formation of sucrose{a icogical Motecules Ea Maltose: It is commonly known as malt sugar. It is an intermediate disaccharide produced during the breakdown of starch and glycogen. Maltose is generally found in germinating seeds. The maltose is formed by the condensation of two a-glucoses. In this reaction, the -OH group at C-1 of one glucose reacts with the -OH group at C-4 of other glucose, liberating a water molecule forming a-1, 4-glycosidic linkage. HOCH, HOCH, HOCH, Hoon a-Glucose a Glucose Maltose, Water 1-1, 4-glycosidic linkage Fig: 2.15: Formation of maltose Lactose: It is commonly known as milk sugar. The lactose is formed by the condensation of B- galactose and B-glucose. In this reaction, the -OH group at C-1 of galactose reacts with the -OH group at C-4 of glucose, liberating a water molecule forming B-1, 4-glycosidic linkage. HoeH, Hos, 4 -Galactose -Glucose Lactose er , . B-1, 4-glycosidic linkage Wat Fig: 2.16: Formation of lactose Ei science Titbits ‘Any carbohydrate which is capable of being oxidized and causes the reduction of other substances without having to be hydrolyzed first is known as reducing sugar, but those which are unable to be oxidized and do not reduce the other substances are known as non-reducing sugars. All monosaccharides and two of three types of disaccharides (maltose and lactose) have the open chemical structure needed to act as reducing agents. The third type of disaccharides, sucrose, and polysaccharides are non-reducing sugars. 2.3.4 Polysaccharides Those carbohydrates which upon hydrolysis yield more than ten monosaccharide units are called polysaccharides. This is largest group of carbohydrates. The polysaccharides which are composed by the condensation of only one kind of monosaccharides are called homopolysaccharides e.g., starch, glycogen, cellulose, chitin; whereas the polysaccharide which are composed by the condensation of different kind of monosaccharides are called heteropolysaccharides e.g., agar, pectin, peptidoglycan. Polysaccharides function chiefly asaz 2 otogicl Molecules food and energy stores, e.g., starch, glycogen, and structural material, e.g., cellulose and chitin. They are convenient storage molecule for several reasons. Their large size makes them more or less insoluble in water, so they exert no osmotic or chemical influence in the cell; they fold into compact shapes and they are easily converted to sugars by hydrolysis when required. Some common polysaccharides e.g., starch, cellulose, and chitin are being discussed here. Starch Starch is a homopolysaccharides which is formed by the condensation of hundreds of a-glucoses. It is storage carbohydrate of plants. It is mainly stored in root, stem and seeds. Cereal grains and potato tubers are rich sources of starch in human diet. Starch is digested in oral cavity and in small intestine by the enzyme amylase. Upon hydrolysis it yields maltose first and then maltose is further digested by maltase enzyme and yields glucoses. The presence of starch in a given sample can be confirmed by iodine test as it gives blue colour with iodine solution. There are two types of starches i.e., amylose and amylopectin eA TD ‘Segment of an amylose molecule BREE aac. ‘Segment of an amylopectin molecule, showing one a-1,6 branch linkage Fig: 2.17: Structure of starches Amylose is un-branched i.e., a linear chain of glucoses in which glucoses are attached together by a-1, 4-glycosidic linkages. It is soluble in hot water only. On the other hand, amylopectin has branched structure i.e., a linear chain of glucoses but more chains of glucoses in the form of branches are also attached by a-1, 6-glycosidic linkages. It is completely insoluble in water. Glycogen Like starch, glycogen is also a homopolysaccharides composed of a-glucoses. It is storage carbohydrate of animals. It is mainly stored in liver and muscles. Therefore it is also known as animal’s starch. The digestion of glycogen is also quite similar to that of starch The presence of glycogen in a given sample can Fig: 248: Stuctro of ayoonen@ 2 Biological Molecules also be confirmed by iodine test as it gives red colour with iodine solution. Structure of glycogen resembles with amylopectin starch but glycogen has much more branching than amylopectin Cellulose Cellulose is most abundant carbohydrate on earth. It is also a homopolysaccharides but unlike starch and glycogen it is formed by the condensation of hundreds of B-glucoses. It is structural carbohydrate of plants as it is major constituent of plant cell wall. Cotton and paper are the pure forms of cellulose. Fig: 2.19: Structure of cellulose Cellulose shows no colour with iodine solution. Structure of cellulose resembles with amylose starch in such a way that it has un-branched structure but it has B-1, 4-glycosidic linkages between glucose residues. ea Science Titbits Cellulose cannot be digested by human body but it has to be taken into diet because it works as roughage or fibre so it prevents abnormal absorption of food in intestine. However, herbivore animals have some symbiotic bacteria that secrete cellulase enzyme for its digestion. Upon hydrolysis it first yields a disaccharide, the cellubiose and then cellubiose is further digested into glucoses. {H,4-lyosicinkages CoH Chitin Lacely group Chitin is the second most abundant organic molecule on earth, It is also a homopolysaccharides. It is a _ structural carbohydrate found in the cell walls of fungi and in the exoskeleton of arthropods. Due to the occurrence of chitin in fungal cell wall, it is also known as fungal cellulose. Chitin is the derivative of N-acetyl glucosamine monomers which is a modified form of glucose. It has an un- branched structure and its monomers are linked together by B-1, 4-glycosidic linkages. Fig: 2.20: Structure of chitin 2.4. PROTEINS Proteins are the main structural components of the cell. All proteins contain C, H, O and N, while some contains P, S. Few proteins have Fe, | and Mg incorporated into the molecule. Glucosamine HoH HW HH 2.4.1 Structure of Proteins Chemically proteins can be defined as polymers of amino acids or polypeptide chains. A protein may consist of a single polypeptide or more than one polypeptide.Amino acids Amino acids are the building blocks of proteins. There are many amino acids known to occur, but only 20 are commonly found in proteins. The amino acids are built on a common plan. Each contains a carbon atom. It is called a alpha) carbon to this a hydrogen atom, an amino group (~ NH2), a carboxyl group (-COOH) and a variable group known as -R group are attached. The R group has a different Fig: 2.21 General structure of an structure in each of the 20 biologically important amino acids amino acid and determines their individual chemical properties. Two simplest amino acids i.e., glycine and alanine are shown in figure 2.21 Dipeptides and Polypeptides Dipeptides and polypeptides are formed by the condensation of amino acids on the ribosome under the instructions of mRNA which takes these instructions from DNA. This process is known as translation. During this process, when an amino acid reacts with another amino acid, the -OH from carboxylic acid group of one amino acid and -H from amino group of other amino acid are liberated and form a water molecule, as a result a bond is established between C of carboxylic acid group and N of amino group of two amino acids called peptide bond. Hence, a product of two amino acids is formed which is known as dipeptide. Catboxyl_ Amino group group Peptide bond H HOH OH Glycine Alanine Glyeylalanine (a cipeptide) Fig: 2.22: Formation of a dipeptide and peptide bond A dipeptide has two ends; one is called amino or -N terminal end while other is called carboxylic acid or —C terminal end. A new amino acid can be added in this chain from its carboxylic acid or -C terminal end in the same way. Thus, a tripeptide (a product of three amino acids) is formed and another water molecule is also released. Similarly, when several amino acids are linked together by many peptide bonds, the polypeptide chain is formed. Structural conformations in proteins A linear polypeptide with a specific sequence and number of amino acids is called primary structure. It is shown by all proteins at the time of their synthesis on ribosomal surface. After synthesis a protein does not remain in its primary structure but can be changed into some other structural conformations (particular form, shape or structure).2 Biological Molecules 43 ‘A helical (a-helix) or flattened sheets (B-pleated sheet) like structures which are established by H-bonding between opposite charge bearing groups of different amino acids are called secondary structures. In some proteins the linear polypeptide is changed into a-helix, then a- helix fold again and again by ionic bonds and disulfide bridges to form a globular shaped structure, the tertiary structure. Some proteins exist in very complex structure in which more than one globule is attached together by hydrophobic interaction. Such structures are called quaternary structures. o> Levels of protein organization poo &, Primary protein structure aaa is sequence of a chain of amino acid aN Pleated sheet Alpha helix Secondary protein structure occurs when the sequence of amino acids are linked by hydrogen bonds Pleated sheet Tertiary protein structure Occurs when certain attractions are present between alpha helices and Alpha helix pleated sheets Quaternary protein structure iS'a proteid Consisting of more than one amino acid chain .23: Structural conformations in proteins 2.4.2 Significance of Amino Acid Sequence Sequence of amino acid in a polypeptide is a characteristic feature of primary structure of protein which is responsible for proper functioning of protein. It is determined by the sequence of nucleotide in DNA. Even due to point mutation (change of single or few nucleotides in DNA) the sequence of amino acid in a particular protein (polypeptide) may be disturbed which causes severe defects in the body as it happens in sickle cell anemia, a hereditary disease.2 biotoical Molecules Normal red blood cells are disc-shaped and look like doughnuts without holes in the centre. They move easily through your blood vessels. Red blood cells contain an iron-rich protein called haemoglobin. This protein carries oxygen from the lungs to the rest of the body. Normal haemoglobin (Hb“) contains four polypeptides i.e. two a-chains which consist of 141 amino acids each and two B-chains which consist of 146 amino acids each. Sickle cell anemia is a serious disorder in which the body makes sickle or crescent shaped red blood cells. Sickle cells contain abnormal hemoglobin called sickle haemoglobin (Hb). Sickle haemoglobin causes the cells to develop a sickle, or crescent, shape. Sickle cells are stiff and sticky. They tend to block blood flow in the blood vessels of the limbs and organs. Blocked blood flow can cause pain and organ damage. Sickle cell anemia is caused by a point (@) Normal amino aid eequence TH Single change nanino seid sequence] Mutation in B-globin gene in ee eee ee) ee which only one nucleotide is ‘ . . T ‘ . . 7 replaced by another which causes a change in amino acid sequence of B-chain of haemoglobin. Sickle cell Sickled. haemoglobin (HbS) shows red blocd only one difference from Hb* ie., glutamic acid is replaced by valine at position number six in B-chain Normal rod blood ells Fig: 2.24: Difference in -chain of Hb* and Hb® 2.4.3 Classification of Proteins Based upon structure and shape proteins can be classified into two groups i.e., fibrous and globular. Fibrous proteins These proteins have fibre or filament like shape. Therefore, they exist in secondary structure during function. These proteins are insoluble in aqueous medium, elastic in nature and cannot be crystalized. Examples are: collagen, fibrinogen, actin, myosin and keratin Globular proteins These proteins have spherical or globules like shape. Therefore, they exist in tertiary or quaternary structure during function. These proteins are soluble in aqueous medium, inelastic in nature and can be crystalized. Examples are: enzymes, hormones, antibodies, channel proteins. 2.4.4 Role of Proteins Proteins are very important molecules in our cells. They are involved in virtually all cell functions. Each protein within the body has a specific function. Some proteins are involved in support or composition of body parts i.e., structural roles, while others are involved in various physiological activities like bodily movement or in defence against germs i.e., functional roles. A list of several types of proteins and their functions is given in table 2.4 and 2.5.KE 2 Biological Molecules Table: 2.4: List of structural proteins Collagen It establishes the matrix of bone and cartilages. Elastin Elastin provides support for connective tissues such as tendons and ligaments. Keratin It strengthens protective coverings such as hair, nails, quills, feathers, homs, and beaks. Histone It arranges the DNA into the chromosome. Table: 2.5 List of functional proteins Enzymes The most of enzymes are protein which control metabolism i.e., they speed up the biochemical reactions. Hormones. ‘Some hormones are protein in nature which are involved in the regulation of physiological activities such as regulation of glucose level, calcium level, digestion, blood pressure ete. Antibodies __| These proteins are produced by WBCs in response to antigen (a foreign particle) and provide immunity. Haemoglobin | It is found in RBCs and is involved in the transport of oxygen mainly and carbon dioxide to some extent. Fibrinogen _| It is found in blood plasma and is involved in blood clotting process. Ovalbumin | Ovalbumin is found in egg whites and casein is a milk-based protein. Both and Casein _| of them are involved in the storage of amino acids. Skills: Analyzing, Interpreting and Communication + Draw table to illustrate different structural and functional proteins with roles of each. 2.5 LIPIDS Lipid is the collective name for variety of organic compounds such as fats, oils, waxes and fat-like molecules (steroids) found in the body. Therefore, it is defined as a heterogeneous group of organic compounds which are insoluble in water (hydrophobic) but soluble in organic solvent such as acetone, alcohol, and ether etc. Lipids are composed of carbon, hydrogen and oxygen as carbohydrates. However, they have relatively less oxygen in proportion to carbon and hydrogen than do carbohydrates. For instance, tristearin is a simple lipid which shows molecular formula as Cs7H110Os. Due to high contents of carbon and hydrogen, they contain double amount of energy than carbohydrates.2 topical Molecules In general lipids are components of cell membranes (phospholipids and cholesterol), act as energy stores (triglycerides), steroid hormones and are also involved in protection, waterproofing, insulation and buoyancy. Some common lipids are acylglycerol, waxes, phospholipids, on 4 on terpenes, prostaglandin and steroids. | foo! | |u| H-C-O7H + H-O;C-C-H # H-C-0-C-C-H + KO Acylglycerol poet The most abundant lipids in y it 4 4 living things are _—_acylglycerol. Chemically, acylglycerols can be defined as esters of glycerol and Fig: 2.25: Esterification fatty acids. An ester is the compound produced as the result of a chemical reaction of an alcohol with acid and a water molecule is released such a reaction is called esterification Metal Ehanvcasd Neb ebercte Glycerol is a trihydroxy alcohol which contains three carbons, each bears an OH group. A fatty acid is a type of organic acid containing one carboxylic acid group attached to a hydrocarbon. Fatty acids contain even number of carbons from 2 to 30. Each fatty acid is represented as R-COOH, where R is a hydrocarbon tail. When a glycerol molecule combines chemically with one fatty acid, a 0 0 monoacylglycerol__(monoglyceride) is, I formed. When two fatty acids combine with a glycerol a diacylglycerol (diglyceride) is formed and when three fatty acids combine with one glycerol. molecule a triacylglycerol (triglyceride) is formed. Triacylglycerols are also called neutral lipid as all three OH groups of glycerol are occupied by fatty acids and no charge bearing OH group is left. Properties and types of fatty acids About 30 different fatty acids are found. Fatty acids vary in length. Acetic acid (2C) and butyric acid (4C) are simplest fatty acid, whereas palmitic acid (16C) and stearic acid (18C) are most common fatty acids. Some properties of fatty acid are increased with an increase in number of carbon atoms, such as melting point, solubility in organic solvent and hydrophobic nature. Some common fatty acids are given in the table 2.6. Fatty acids are either saturated or unsaturated. Fatty acids in which all of the internal carbon atoms possess hydrogen side groups are said to be saturated fatty acids because they contain the maximum number of hydrogen atoms that are possible, e.g., palmitic acid. Saturated fatty acids tend to be solid at room temperature (higher melting point) and are more common in animal lipids (fats). Il -C—OH HO|-C-R H-C—O-C—-R | e |g H-C—OH +HO|—-C—R—*H-C—O—C—R +3H,0 ie e | ¢ OH HO|—-c-R H-C—O—-C—R H, Glycerol Fatty acids Tracy glycerol Water Fig: 2.26: Formation of a triacylglycerol (neutral lipid){a icogical Motecules Unsaturated fatty acids have one or more pairs of carbon atoms joined by a double bond. They therefore are not fully saturated with hydrogen, e.g., oleic acid. Unsaturated fatty acids are liquid at room temperature (lower melting point) and are more common in plant lipids (oils). Triglycerides containing hydrocarbon chains melt at a low temperature. This is useful for living things. Table: 2.6: Common types of fatty acids Saturated spaimive | Mastlaisand Tag | crs (cry Coon e stewie [Mestlawand [aq | cry (cHajn COOH 7 eral 30Wic —_[oveot [ie __| CHa Ray HCH |Rnv COOH 7 “noise | Vegetani ota [18 | oFa (O%p,GH —OHOHLOH OH oray COOH 5 Waxes Waxes are highly hydrophobic compounds. There are two types of waxes. Natural waxes are simple lipids. They are typically esters of long chain fatty acids and long chain alcohols, such as bee's wax (found in honeycomb) and cutin (on leaf surfaces of plants). These are chemically inert and resistant to atmospheric oxidation. Waxes have protective functions in plants and animals. Synthetic waxes are generally derived from petroleum or polyethylene e.g. paraffin wax which is used to make candles. Phospholipids Phospholipids are derived _from phosphatidic acid, A phospholipid is formed when phosphatidic acid combines with one of i the four organic compounds such as choline 12 (@ nitrogenous base), ethanolamine (an amino alcohol), inositol (an amino alcohol) and serine (an amino acid). A phosphatidic acid molecule is most similar to diglyceride that it contains a glycerol, two fatty acids esterified with first and second OH groups of glycerol and a phosphate group esterified with * third OH group of glycerol. Most common type % of phospholipid is phosphatidylcholine also called lecithin in which choline is attached to phosphate group of phosphatidic acid. One Fig. 2.27: Phosphatidyichoine (Lecithin) end of the phospholipid molecule, containing the phosphate group and additional compound is hydrophilic ie., polar and readily soluble in water. The other end, containing the fatty acid side2 iotogica Molecules chains, is hydrophobic i.e., non-polar and insoluble in water. These phospholipids are major constituents of lipid bilayer of cell membrane. cH, Terpenes at cl All the terpenes are synthesized from a five-carbon building block H,c~ ~¢~~"? known as isoprene unit. This unit condenses in different ways to form I many compounds. Two isoprene units form a monoterpene e.g., H menthol, four form a diterpene e.g., vitamin A, phytol (chlorophyll tail) Fig. 2.28 Isoprene unit anq six form a triterpene e.g., ambrein. Natural rubber is a polyterpene. Steroids Steroids are lipids of high molecular weight which can be crystalline. A steroid nucleus consists of 17 carbon atoms arranged in four attached rings, three of the rings contain six carbon atoms, and the fourth contains five. The length and structure of the side chains that ie extend from these rings distinguish one steroid from other steroids. These structures are synthesized from isoprene units. Cholesterol is a structural component of cell membrane. Cholesterol is the precursor of a large number of equally important steroids which include the bile acids, male sex hormone testosterone, female sex hormone progesterone and estrogen etc. Bile salts which emulsify fats and Vitamin D, which helps to regulate ploi2z2 Seo ie) calcium metabolism are also steroid. Prostaglandins Prostaglandins exist in virtually every mammalian tissue, acting as local hormones. Prostaglandins are derived from arachidonic acid. Their functions vary widely depending on the tissue. Some reduce blood pressure, whereas others raise it. In the immune system, various prostaglandins help to induce fever and inflammation and also intensify the sensation of pain. They also help to regulate the aggregation of platelets an early step in the formation of blood clots. In fact, the ability of aspirin to reduce fever and decrease pain depends on the inhibition of prostaglandin synthesis. Science, Technology and Society Connections + Relate the role of prostaglandin in inflammation with the inhibition of prostaglandin synthesis through aspirin. Prostaglandins play a pivotal role in inflammation a process characterized by redness (rubor), heat (calor), pain (dolor), and swelling (tumor). The changes associated with inflammation are due to dilation of local blood vessels that permits increased blood flow to the affected area. The blood vessels also become more Permeable, leading to the escape of white blood cells (leukocytes) from the blood into the inflamed tissues. Aspirin is antiinflammatory, analgesic, and antipyretic. Aspirin inhibits prostaglandin synthetase salicylate. This drug affects the metabolism of arachidonate via the lipoxygenase pathway by inhibiting the conversion of ‘12-hydroperoxy- to 12-hydroxy-5, 8, 10, 14-eicosatetraenoic acid.@ 2 Biological Molecules 2.6 NUCLEIC ACID Nucleic acids were first reported (in 1869) by a Swiss physician when he isolated a new compound from the nuclei of pus cells (white blood cells). This compound was neither a protein nor lipid nor a carbohydrate; therefore, it was a novel type of biological molecule. He named this molecule as nuclein, because it was located in the nucleus. The basic structure and chemical nature of nuclein was determined (in 1920) and was renamed as nucleic acid because of its acidic nature. 2.6.1 Chemical Structure of Nucleic Acids Now it has been cleared that nucleic acids are of two types i.e., deoxyribo nucleic acid (DNA) and ribo nucleic acid (RNA). Both nucleic acids are linear un-branched polymers. The monomers of the nucleic acid are called nucleotides. Composition of a nucleotide Nucleotides of DNA are called deoxyribonucleotides and of RNA are known as ribonucleotides. Each nucleotide consists of pentose sugar, a phosphate and a nitrogen containing ring structure called base. The pentose sugar in deoxyribonucleotides is en, 2. HOCH, OX on een er ar NE wes K 4" on tH bu be Deoxyribose Ribose j Fees a (found in RNA) Phosphoric acid a ° ° H Il Il Cc cS c és Z Z Zz 2 CHa NI Sen NE 30 Ng ee Hg 3c HC2 , 8CH aan 92 4 SPH 02 , §CH Sh o7 eal of ee ad H H H Pyrimidine Cytosine (C) Uracil (U) Thymine (T) (found in RNA) (found in DNA) (NH ° H Cc c. c. Z N Z N NZ Pom i aE Hn Se tl gen x all gen Uo al HC. Cus H 2 c Kaen aoe SN Kaen H H H Purine Adenine (A) Guanine (G) Fig. 2.30: Components of nucleotides@ 2 Biological Molecules deoxyribose and in ribonucleotides is ribose. Phosphoric acid is a common component of both nucleotides which provides acidic properties to DNA and RNA. The nitrogen containing ring structures are called bases because of unshared pair of electron on nitrogen atoms, which can thus acquire a proton There are two major classes of nitrogenous bases i.e., single ring pyrimidine and double ring purines. Pyrimidine bases are of three types i.e., cytosine (C), thymine (T) and Nitrogenous base NH, 7 ¢ oY) "Phosphate group 8 | 2 Pa N~ 4 SN 9 3 ‘CH. 3h. 4 F 2' . 7 OH in RNA OH RS Hin DNA Sugar Fig, 2.31: Structure of a nucleotide uracil (U). Thymine is only found in DNA while the uracil is only found in RNA. On the other hand, the purine bases are also of two types i.e., adenine (A) and guanine (C). During the formation of a nucleotide, first nitrogenous base is linked with 1' carbon of pentose sugar. Such combination is called nucleoside. When a phosphoric acid is linked with 5! carbon of pentose sugar of a nucleoside, the nucleotide is formed. A nucleotide with one phosphoric acid is called nucleoside monophosphate with two phosphoric acids is called nucleoside diphosphate and with three phosphoric acids is called nucleoside triphosphate. The nucleotides which take part in the formation of DNA or RNA must contain three phosphates but during their incorporation into DNA or RNA polymer each nucleotide losses its two terminal phosphates. Different terms used for nucleosides and nucleotides are given in the table 2.7. Tabi : Different types of nucleosides and nucleotides of RNA and DNA. Ribonucleosides | Ribonucleotides Deoxyribonucleosides | Deoxyribonucleotides (Ribose + Base) | (Ribose+Base+ —_| (Deoxyribose + Base) | (Deoxyribose+Base+ Phosphate) Phosphate) ‘Adenine Adenosine AMP, ADP, ATP. d-Adenosine dAMP, dADP, dATP ‘Guanine Guanosine GMP, GDP, GTP’ d-Guanosine GMP, dGDP, dGTP Gyiosine cytidine CMP, CDP, CTP | d-Cyliine ‘dCMP, dCDP, dCTP Uracil Thymine | Uredine UMP, UDP, UTP | d-Thymidine TMP, dTDP, aT@ 2 Biological Molecules Enz Polymerization of nucleotides (Formation of polynucleotide) Nucleotides are also joined together by a condensation reaction like other biomolecules. Unlike proteins, carbohydrates, and lipids, however, the molecule that is released is not water but pyrophosphate (two phosphate groups bound together). When pyrophosphate is cleaved by the addition of water, a great deal of free energy is released which derives the process. In this way nucleotides begin to link by phosphodiester bonds and a polymer of nucleotides (polynucleotide) is formed. Polynucleotides have a free 5' phosphate group at one end and a free 3° hydroxyl group at the other end. By convention, these sequences are named from 5' to 3’, |e" a. = = ae eo ‘Send eo = Send \ y ou Fig. 2.32 Polymerization of nucleotides 2.6.2 Chemical Nature and Role of ATP and NAD Adenosine triphosphate (ATP) is a mononucleotide. As shown in fig. 2.32 ATP has three parts, connected by covalent oe Sy bonds: (a) adenine, a nitrogen base, (b) -f Ny “4 ribose, a five carbon sugar, (c) three phosphates. The two covalent bonds linking Fe Adenine the three phosphates together are called Phosphate groups. high-energy bonds. ATP can be converted OH oH to ADP and inorganic phosphate (iP) by Ribose hydrolysis. ATP is known as the energy ‘Adenosine ‘Rdenosine monophosphate ‘Adenosine diphosphate Nicotinamide adenine dinucleotide ‘Adenosine biphosphate (NAD) consists of two nucleotides. One Fig. 2.33 Structure of ATP currency of cells.2 Biological Molecules 9 , ( Sy NH? el On OH uy, yA N a C13 on Wy attic OH OH Fig. 2.34 Structure of NAD The width of duplex is 2nm nucleotide consists of nicotinamide, sugar and phosphate. Other nucleotide consists of adenine-sugar and phosphate. The two nucleotides are joined by their phosphate group forming a dinucleotide. NAD is a coenzyme. 2.6.3 Watson and Crick Model of DNA In 1951, Erwin Chargaff found that the nitrogenous bases in a DNA show specific ratios. He observed that amount of adenine is always equal to the amount of thymine and amount of guanine is always equal to the amount of cytosine in DNA. This implies that the total purines and total pyrimidines are in 1:1 in any DNA. This conclusion is known as Chargaff’s tule. In those days the X-ray diffraction analysis of DNA by Maurice Wilkins and Rosalind Franklin was published. They first time claimed that DNA is a duplex (double helix) molecule. while the length of each tum is 3.4nm. In 1953, on the basis of these observations a graduate student Francis Crick and a research fellow James Watson of Cambridge University proposed a physical model of DNA which is now called Watson and Crick Model of DNA. According to this model a DNA is made up of two polynucleotide chains which are attached together by base pairs. In order to make base pairing the two polynucleotide chains are opposite in direction i.e ‘one chain runs from 5' to 3’ downward and the other chain runs {a) Key features of double helix model {b) Partial chemical structure Fig. 2.35 Watson and Crick model of DNA@ 2 Biological Molecules from 5’ to 3’ upward. Both chains show a constant width of 2 nm. Therefore, both chains are supposed be antiparallel to each other. The base pairing is very specific i.e., Adenine makes the pair with Thymine and Guanine with Cytosine. The base pairs are held together by the hydrogen bond. There are three hydrogen bonds between Guanine and Cytosine and two hydrogen bonds between Adenine and Thymine. Each tum of the duplex consist of 10 base pairs. Both polynucleotide chains are complementary to each other. There is no restriction of the sequence of nucleotides along the length of a DNA strand. The sequence can vary in countless ways. The sequence is specific for different species, organisms and even individuals. Hill science Titbits Watson and Crick assembled the molecular model and published their two-page article on their molecular model of DNA in the journal “Nature in April 1953. Few milestones in the history of biology have as broad an impact as their double helix. They were awarded Nobel Prize in 1962 for their model of DNA. 2.6.4 Concept of Gene A gene is region of DNA which is made up of nucleotides. It is the physical and functional unit of heredity. Each gene contains the information required to build specific proteins needed in an organism, such as they contain the instructions for our individual characteristics — like eye and hair colour. In order to make proteins, the gene from the DNA is copied into messenger RNA. The mRNA moves out of the nucleus and uses ribosomes to form the polypeptide that finally folds and configures to form the protein. 2.6.5 Ribonucleic Acid (RNA) RNA is also a polymer of nucleotides. Its detailed chemical nature has already been discussed in previous topics. Unlike DNA, the RNA is generally single stranded and does not form a double helix like DNA. However, some regions of RNA shows a secondary double stranded structure in their complementary regions. There are three major classes of RNA each with a special function in protein synthesis. These RNA are transcribed from DNA template. Messenger RNA (mRNA) MRNA consists of a single strand of variable length. Its length depends upon the size of the gene, as well as the protein for which it is taking message. For example, for a protein molecule consisting of 100 amino acids, the mRNA will have the length of 300 nucleotides. Actually every three nucleotides in mRNA encode a specific amino acid, such triplets of nucleotides along the length of mRNA are called codons of genetic codes. mRNA is about 3 to 4% of the total RNA in the cell. mRNA takes the genetic message from the nucleus to the ribosome in the cytoplasm to form particular protein. This process is known as translation& p Bisosica Molecules Ribosomal RNA (rRNA) Ribosome consists of rRNA and protein. rRNA is transcribed by the genes present on the DNA of the several chromosomes. It is called rRNA because it eventually becomes part of ribosome. The rRNA is packaged with a variety of proteins into ribosomal subunits. The base sequence of rRNA is similar from bacteria to higher plants and animals. RNA have largest size among the RNA. Approximately, 80% of total RNA contents of a cell are rRNA. It is a part of ribosome where protein synthesis takes place. In other words rRNA provides a platform for protein synthesis. Transfer RNA (tRNA) It is the smallest of the RNA molecules and it consists of 75 to 90 nucleotides. A tRNA is one a single stranded molecule but it shows a duplex appearance at its some regions where se complementary bases are bonded to one another. It shows a flat cloverleaf shape in two voor dimensional views. Its 5! end always terminates in Guanine base while the 3/ end is always terminated with base sequence of CCA. Amino acid is attached to tRNA at this end. The "5" nucleotide sequence of the rest of the molecule MootitootBbescoot is variable. Fig: 2.36: Cloverleaf model of (RNA tRNA has three loops. The middle loop in all the tRNA is composed of 7 bases, the middle three of which form the anticodon; it is complementary to specific codon of mRNA. The D loop recognizes the activation enzyme. Theta (0) loop recognizes the specific place on the ribosome for binding during protein synthesis. There is at least one tRNA molecule for each of the 20 amino acids found in proteins. Sixty tRNA have been identified. However, human cells contain about 45 different kinds of (RNA molecules, each transports a specific amino acid from cytoplasm to the surface of ribosome for protein synthesis. ‘Science, Technology and Society Connections + Correlate the scanning tunnelling microscope as the latest advancement for seeing the atoms of DNA. The Scanning tunneling microscope was invented in 1980. It can allow scientists to view atoms on the surface of a solid. It is a very powerful tool that can be used to resolve features less than a nanometer. The microscope's inventors, Gerd Binnig and Heinrich Rohrer were awarded Nobel Prize in Physics in 1986, Seeman’s group worked on the DNA |scanning tunneling| Atoms seen on the eo ae eee ease atitacatorataoldl IN at{a icogicat Motecules 2.7 CONJUGATED MOLECUELS Molecules when joined by other kinds of molecules are called conjugated molecules. The examples are glyocolipids, glycoproteins, lipoproteins and nucleoproteins, Glycolipids are complex lipids containing one or more simple sugars in connection with long fatty acids or alcohol. Glycolipids are present in white matter of brain and myelin sheath of nerve fibres and chloroplast membrane. Glycoproteins are formed when proteins are covalently attached to carbohydrates. Glycoproteins are widely distributed in the cells. They function as hormones, transport proteins, structured proteins and receptors. The blood group antigens contain glycoproteins, which also play an important role in blood grouping Lipoproteins are formed by the combination of protein with phospholipids. Phospholipid protein Why do the nucleotides in DNA have a complexes are widely distributed in plant and animal | jyarogen atom at the 2 carbon instead of the material. They occur in milk, blood, cell nucleus, egg | hydroxyl group in ribose? The answer is that a yolk membrane and chloroplasts of plants. hydroxyl group at the 2' position can participate in i a reaction that cleaves the phosphodiester bond. Nucleoproteins consist of simple basic | Thus, DNA can act as a stable. long-term protein and nucleic acid. They are found in | repository for genetic information. RNA is usually chromosomes and ribosomes. degraded within your calls in 30 minutes. cience Titbits ‘Skills: Analyzing, Interpreting, and Communication + Draw the Watson—Crick model of DNA + Illustrate the formation of phosphodiester linkage ‘Sclonce Technology and Society Connections ‘+ List the career opportunities in the field of biochemistry. Biochemistry, the study of chemical processes that take place in living organisms, is a broad field that offers a wide range of career options. Biochemists can pursue stem cell or genetic research that has the potential to result in dramatic medical or scientific breakthroughs. Some biochemists study the body's immune response to germs and allergens or the effectiveness of drugs in treating a wide array of affictions. Other biochemists ‘work in the commercial food or agricultural field looking for ways to improve products and crops. The many and diverse applications of biochemistry include pharmacology, genetics, immunology, bioinformatics, environmental science, forensics, toxicological studies and food science. The career options are nearly endless, and still unfolding, as new applications for this exciting field of study continue to evolve. rte Ly 1. Performing Benedict's test for reducing sugars and confirmation of the presence of starch through Iodine test Confirmation of the presence of proteins through Biuret test Confirmation of the presence of lipids through Emulsion test Demonstration of the presence of nucleic acids in biological materials e.g., oniongz 2 Biological Molecules S om 1. Select the correct answer OS NH, Cc COOH i® (i) Anamino acid molecule has the following structure: Which two of the groups combine to form a peptide link between two amino acids? (A) 4 and 2 (8) 4 and3 (C) 2and3 (0) 2and4 (i) Which class of molecule is the major component of cell membrane (A) phospholipid (8) cellulose (C) wax (D) triglyceride (i) Glycerol is the backbone molecule for (A) ATP (B) terpenes (C) neutral lipids (0) steroids (iv) A fatty acid is unsaturated if it (A) contains hydrogen (B) contains double bonds (C) contains an acid group (D) all of them (v)__ InRNA the nitrogen base that takes the place of thymine is (A) adenine (B) cytosine (C) guanine (D) uracil (vi) The ending—ose means a substance is a (A) sugar (B) lipid (C) protein (O) nucleic acid (vii) Glycolipids and lipoprotein are important components of (A) cellularmembrane —_(B) cell wall (C) both of them —_(D) none of them (vill) When two amino acids are linked to form peptide linkage is removed (A) hydroxyl (B) water (C) carbon (0) nitrogen (ix) Whatis the theoretical number of chemically different dipeptides that may be assembled from two amino acids? (A) one (B) two (C) three (0) four (x) Apolar molecule is in water (A) soluble (B) insoluble (C) reactive (0) innert@ 2 Biological Molecules (xi) Which statement correctly describes a property of water? (A) a relatively large amount of heat is needed to increase its temperature (B) at normal room temperature, its molecules are bound together by ionic bonds (C) the highest density of water occurs below its freezing point (D) water acts as solvent for nonpolar molecules (xii) Estrogen, vitamin-D and cholesterol are all examples of (A) glycolipids (B) lipoproteins (C) terpenes (D) steroids (xiii) Which term includes all others? (A) carbohydrate (B) starch (C) monosaccharide (0) polysaccharide (xiv) Choose the pair of terms that correctly completes this sentence: Nucleotide are to iS -are to proteins. (A) nucleic acids; amino acids {B) amino acids; polypeptides (C) glycosidic linkages; polypeptide linkages (D) polymers; polypeptides (xv) The enantiomer of D-glucose is (A) D-galactose (B)L-galactose (C) both of them —_(D) none of them ®) How would you describe biochemistry? What are bioelements? Describe the chemical composition of protoplasm. 2 3. 4 5. What are the four fundamental kinds of biological molecules? Explain. 6. Whyis the covalent bond in water polar? 7. Why water is regarded as universal solvent? 8. Whatis the importance of hydrogen bonding? 9. Why very large amount of heat can increase very little temperature in water? 10. How water protects living things against sudden thermal change? 11. Whatiis the importance of high heat of vapourization of water to animals? 12. Describe classification of carbohydrates. 13, Describe the classification of monosaccharides? 14. Describe the conversion of open chain of ribose into ring chain. 15. Draw and label the ring forms of alpha and beta glucose. 16. Justify that the laboratory-manufactured sweeteners are “left handed” sugars and cannot be metabolized by the “right handed” enzymes.gz 2 Biological Molecules 47. 18. 19, 20. a 22. 23. 24. 25. 26. 27. 28. 29. (a) (b) (©) (d) (e) ) (9) (h) 0} 0) (kK) w (m) Illustrate the formation and breakage of (a) sucrose (b) maltose (c) lactose. Draw the structural formula of amino acid. Describe the synthesis of peptide bond Describe the four types of structure of proteins. Describe (a) globular proteins (b) fibrous proteins. Describe the classification of lipids What role do lipids play in living organisms? Why phospholipids form a thin layer on the surface of an aqueous solution? What is isoprene unit? Explain. Describe a steroid nucleus. How might an error in the DNA of an organism effect protein function? Define gene is a sequence of nucleotides as part of DNA, which codes for the formation of a polypeptide. Write the differences between: major and minor bioelements dimer and polymer polar and nonpolar covalent bond polyhydroxy aldehyde and polyhydroxy ketone alpha and beta glucose D-glucose and L-glucose amylase and amylopectin amylopectin and glycogen primary and secondary structure of proteins tertiary and quaternary structure of proteins purine and pyrimidine saturated and unsaturated fatty acids DNA and RNA Fe] Extensive Questions 30. 31 32. Describe the chemical composition of protoplasm Distinguish carbohydrates, proteins, lipids and nucleic acids as the four fundamental kinds of biological molecules. Describe and draw sketches of dehydration synthesis and hydrolysis reactions for making and breaking of macromolecule polymers.@ 2 Biological Molecules 33. 34. 35. 36. 37. 38. 39. 40. 4 42. 43. 44, 46. 46. 47. 48, 49. 50. 51 52. 53. How the properties of water make it the cradle of life? Distinguish the properties and role of monosaccharides. Write the emperical formula of monosaccharides and classify them. Compare the stereoisomers of glucose. Distinguish the properties and role of disaccharides. Describe glycoside bond in the transport of disaccharides. Distinguish the properties and role of polysaccharides. Describe the properties and roles of starch, glycogen, cellulose and chitin. Justify the significance of the sequence of amino acids through the example of sickle cell haemoglobin List examples and the roles of structural and functional proteins. Describe the properties and roles of: (a) acylglycerol (b) phospholipids (c) terpenes (d) waxes Evaluate the role of the following as important groups of lipids and describe their roles in living organism: {a) steroid (b) prostaglandins Describe the molecular level structure of nucleotides. Distinguish among the nitrogenous bases found in the nucleotides of nucleic acids. Describe the structure of a mononucleotide (ATP) and a dinucleotide (NAD). Explain the formation of phosphodiester bond. Explain the double helical strucutre of DNA as proposed by Watson and Crick. What is a gene? How gene codes for the formation of a polypeptide? Explain general strucutre of RNA. Explain the structure and role of three types of RNA. Describe the roles of the following conjugated molecules: (a) glycolipids () glycoproteins (©) lipoproteins (d)_nucleoproteins