0 Biomolecules POINTS TO REMEMBER 1. Biomolecu Macromolecules which are naturally occurring in biological systems are called biomolecules. Examples: polysaccharides (starch, cellulose, etc.) proteins, enzymes, vitamins, hormones, etc. 2. Carbohydrates: These are optically active polyhydroxy aldehydes or ketones or the compounds which proluce such units on hydrolysis, e.g. glucose, sucrose, cellulose, starch, etc. 3. Classification of carbohydrates: (@) Monosaccharides: The simple carbohydrates that cannot be broken further into smaller m hydrolysis, e.g, glucose and fructose, ribose, etc (6) Oligosaccharides: These are the carbohydrates which on hydrolysis give two to ten units of monosaccharides, e.g. sucrose, maltose, raffinose, stachyose, etc. (©) Polysaccharides: These are the carbohydrates which produce a large number of monosaccharide units ‘on hydrolysis, e.g, starch, cellulose, etc Importance of carbohydrates: (8 Carbohydrates act as biofuel to provide energy for functioning of living systems. on CoHi205 + 60; —~ 6CO, + 6H,O + 2832 KI Gi) Carbohydrates are used as storage molecules as starch in plants and glycogen in animals. (ii) D-Ribose and 2-Deoxy-D-ribose are present in RNA and DNA, respectively. (iv) Cellulose acts as structural material of cell walls of bacteria and plants. (») Carbohydrates provide raw material for many important industries like textiles, paper, lacquers and breweries. 1 2 Fe S| n 4 e) z) ma x i S ee) m ye) 4, @ Reducing sugars: Those carbohydrates which contain free aldehydic or ketonic group and reduce Fehling’s solution and Tollens’ reagent are called reducing sugars, e.g., all monosaccharides, maltose and lactose. (ii) Non-reducing sugars: Those sugars which do not have free aldehydic or ketonic group and do not reduce Fehling’s solution or Tollens’ reagent are called non-reducing sugars, ¢.g., sucrose, 5. Preparation of Glucose (@) From sucrose: CyHnO, + HO —H + CeH2Os + Cots(&) From starch: Commercially, glucose is obtained by hydrolysis of starch by boiling it with dil, H,SO, at 393 K under pressure. (CHjOs), + 2H,0 Sach of sone Bake sam MCE ‘Gace 6. (@) Structure of Glucose: Glucose is a six carbon straight chain aldose which has one aldehydic group (CHO), one primary hydroxyl group (—CH,OH) and four secondary hydroxyl groups (—CHOH), Ifthe —OH group attached to C-S is on the right side, the glucose is dextrose sugar Le., dextrorotatory and assigned as D-configuration; if the —OH group attached to C-5 is on the left side, it is assigned L-configuration. The (+) and (~) signs represent the optical rotation as dextro and laevo, respectively and have no relationship with D and L. configuration CHO CHO H——OH HO—j—H Ho—}—H n—-on cHo n—t_on cHo | HO} HoH non one a HOA Gon hon enon CHhy—on Dierdyeniitnde —D-G}Oeme LO Ayeenlddnde LCs (©) Cyelic structure of glucose: The glucose has been shown to possess cyclic structure represented as follows: ° 4 ° = a $CH,0H SCHOH *CH.0H e-D(4) Gow BD-GGhco8e Haworth Structures sCH,OH ©. F he Ji on Hu SI) 2| 4 ou D4 Glucopyranose B-D-(4-GtucepyranoseReactions of Glucose (CHOH Glucose eyanchydrin [re coon CHO | (CHOH), 28S. (CHOH)s. = (CH,—CH)—CH»—CH>— ‘lexane coon CH0H soca id tee an 3 e coo# cHon—6n 3 (CHOW), ' 3 (CHOW. = CH;OH cuca CH.OH CHO I Giucose oxime ceo cr. | cr,—o—C_cn, (Glucose pentasceate 8. Structure of Fructose: Fructose is a ketohexose and has the molecular formula CgH,,Og, It belongs to Daseries and is a laevorotatory compound. a fi it] no e—t208 nowje—c—_on ‘1 3 notin no—|—n | 0 4 4 e HOH a t}—on ( 4 \ 5| iH iH. a. ql ‘CHO ‘CH20H_ Fran e-D46)-Fructofuranose BD }-Fructofuranose The cyclic structures of two anomers of fructose are represented by Haworth structures as given below. 4 6 °. CHOH = HOHC OH é 2 \ Hl on XH on/ H\L 3p on H\ Ia 3//” CHOW }—_Y¥ ¥—4 7 OH OH OH OH -D--)-Fructofuranoee B.D-C)-Fructouranose 9. Disaccharides: The sugar which on hydrolysis gives two units of monosaccharides is called disaccharide. Disaccharides are crystalline solids and are soluble in wate. Sucrose, maltose and lactose ate disaccharides Hydrolysis of sucrose is called inversion of cane sugar. Sucrose is a disaccharide because on hydrolysis, it produces two monosaccharides namely D-(+)-giueose and D--)-fructose CiHnO + HO —— — CgHrOg + CoHhi20¢ Same D-@-Gcoe D9 Feane (eoxsere) (monnacchde) (rena)(@) Ring structure of a sucrose molecule: A sucrose molecule is composed of a-glucose and Befructose units. H OH e-D-Glucose (6) Ring structure of a maltose molecule: A maltose molecule is composed of wo a-D-glucose units in which C-1 of one glucose (I) is linked to C-4 of another glucose unit (I). 8 6 CH,0H CH20H ©, 5 5 " ie i Se on on HY Ns aaj / OH é H on H oH a (6) Ring structure of a lactose molecule: A lactose molecule is composed of -D-galactose and B-D-glucose units. a, «, H,08 Cx:0H js, ©. " fk SN WAT pH \OH HY) o on HY HN 2//H Ns 2 I HoH HOW f-D.Gataee BeD-Ghucse Lactose 10. Polysaccharides: Polysaccharides are the carbohydrates which yield a large number of monosaccharide ‘molecules upon hydrolysis. Starch, cellulose and glycogen are examples of polysaccharides. (@ Starch: The fundamental unit of starch is a-D-glucose. Structure of starch: Starch is a polymer of a-glucose and consists of two components—amylose and amylopectin. Amylose is a long unbranched chain with 200-1000 o-D.(+)-glucose units held by C1-C4 glycosidic linkage. chon CH;0H 0. H H/H nt sk 1 on on n/Do~4 " HOH tisk ante ee Amylopectin is a branched chain polymer of a-D-glucose units in which the chain is formed by C1-C4 slycosidic linkage, whereas branching occurs by C1-Cé glycosidic linkage.CHO 4,08 yes pas H Link Link Amlopectin (6) Cellulose: Cellulose is a polysaccharide. The fundamental structural unit of cellulose is B-D-glucose. Structure of cellulase: Cellulose is a linear polymer of D-glucose which are joined by glycosidic linkage between C1 of one glicose unit and C4 of the next glucose unit. HOHC 0, 4 yf Y S OH HOH.C 6 ou oO fo \ oH HOHSC é Ser 0, / \ rinks OH o Y/Y Cetatose 11. Amino acids: Those compounds, whose molecule contains both the carboxylic acid group and the amino roup are called amino acids. There are twenty amino acids which form protein. The amino acids which are synthesised in body are known as non-essential amino acids, e.g., glycine, alanine. Those amino acids ‘which cannot be synthesised in body and must be obtained through diet are known as essential amino acids, e.g. valine, lysine, ‘Amino acids have also been classified as neutral, acidic and basic amino acids. Amino acids like glycine, valine, ete. which contain one —NH, and one COOH group are called neutral amino acids. Those amino acids such as aspartic acid, glutamic acid, ete. which contain one —NHs group and two —COOH groups ate called acidic amino acids and amino acids such as lysine, histidine, etc., which contain two —NH, ‘groups and one —COOH group are called basic amino acids 12. Proteins are complex nitrogenous organic molecules which are essential for growth and maintenance of by. Chemically, proteins are the polymers of a-amino acids which are linked by peptide bonds (—C—NH—)(@) Types of proteins based on molecular shape: (@ Fibrous proteins: They have thread-like molecules which tend to lie side by side to form fibres, e., keratin, collagen, myosin, ibroin, etc. In such proteins, the molecules are held together by hydrogen and disulphide bonds. They are insoluble in water. They are the chief structural materials of animal tissues, i) Globular proteins: They have molecules which are folded into compact units that often form spheroidal shapes. The area of contact between molecules are small and inter-molecular forces are comparatively weak, e.¢.. insulin, thyroglobulin, albumin, haemoglobin and fibrinogen. In clotting of blood, fibrinogen gets converted into fibrous protein, fibrin. () Structure of Proteins: There are four levels at which the staicture of proteins are studied. These are primary, secondary, tertiary and quarternary levels. (@ Primary structure of proteins: The sequence in which various amino acids are arranged in a protein is called its primary structure, Any change in the sequence of amino acids creates different protein which alters biological functions. (i Secondary structure of proteins: It refers to shape in which a long polypeptide chain exists. A protein may assume a-helix structure or B-pleated sheet structure. The d-helix structure results due to regular coiling of polypeptide chain which is stabilised by intramolecular hydrogen bonding. Keratin in hair, nails, wool and myosin in nucleus have a-helix structure, In B-pleated sheet structure, all peptide chains are stretched to nearly maximum extension and then arranged side by side and held together by intermolecular hydrogen bonding. Silk has P-pleated sheet structure, Gi) Tertiary structure of proteins: The tertiary structure of proteins represents overall folding of the polypeptide chain, e., further folding ofthe secondary structure. It gives rise to two major molecular shapes, viz. fibrous and globular. The main forces which stabilise 2° and 3° structures of proteins are hydrogen bonds, disulphide linkages, van der Waals forces and electrostatic force of attraction. () Quaternary structure: Some of the proteins are composed of two or more polypeptide chains referred to as sub-units. The spatial arrangement of these subunits with respect to each other is known as quaternary structure (©) Denaturation of Proteins: When a protein in its native form is subjected to a change, such as change in temperature or change in pH, the hydrogen bonds are disturbed. Due to this, globules unfold and helix get uncoiled and protein loses its biological activity. This is called denaturation of protein. During denaturation, 2° and 3° structures are destroyed but 1° structure remains intact, e.¢., coagulation of egg while on boiling, cudling of milk, ete 13. (@) Enzymes: Enzymes ate essential biological catalysts which are required to catalyse biological reactions, e.g., maltose, lactose, invertase, etc. Almost all the enzymes are globular proteins. (b) Oxidoreductase enzymes: Enzymes which catalyse the oxidation of one substrate with simultaneous reduction of another substrate. (©) Phenylketonuria: Disease caused by deficiency of the enzyme phenylalanine hydroxylase. (@) Albinism: Disease caused due to deficiency of an enzyme tyrosinase. (©) Streptokinase: Enzyme which dissolves the blood clot formed in coronary artery which leads to heart trouble. 14, Nucleic Acids: Nucleic acids are long chain polymers of nucleotides. They play an important role in transmission of hereditary characteristics and biosynthesis of proteins. ‘Types of nucleic acids: There are two types of nucleic acids. These are DNA and RNA. (a) Constituents of nucleic aci () Pentose sugar (i) Phosphoric acid (tit) Nitrogenous bases. In DNA, B-D-2-deoxyribose sugar is present while in RNA B-D-ribose sugar is present. Nitrogen containing bases: There are two types of nitrogen containing bases found in nucleic acids. ‘These are pyrimidines and purines. Pyrimidines: There ate three bases derived from pyrimidines. These are cytosine (C), thymine (T) and uracil (U). In DNA, thymine (T) is present but in RNA, uracil (U) is present. Purines: There are two bases derived from purine. ‘These are adenine (A) and guanine (G),‘Nucleoside: A unit formed by the attachment of a base to |'-position of sugar is known as nucleoside. HO—HIC8 Base OH OH Nucleotide: When nucleoside is linked to phosphoric acid at 5'-position of sugar moiety, the unit obtained is called nucleotide. oP. \ 1 H yo / Hu on On Nucleotides are joined together hy phosphodiester Tinkage between 5° and 3° carbon atoms of the pentose sugar 9 Be o-P—o—cH, Prosphadicter | gz poo nkage { ° ° Base 0-P-0—CHt0. 2 CHly 0, Suna on 3 end of chain Formation of dinucleotide () Deoxyribonucleic acid (DNA): It contains a pentose sugar deoxyribose, and adenine, guanine, thymine and cytosine bases. A phosphate group is present at C-5 of the sugar unit. The repeating units, deoxyribonucleotides, are linked by phosphate group. Thus, they are the biopolymers of deoxyribonucleotides and have double helix structure of polynucleotides. The wo strands of DNA are said to be complementary to each other. Adenine forms hydrogen bonds with thymine whereas cytosine forms hydrogen bonds with guanine, They are responsible for genetic characteristics and for sending information and instruction in the cell for the synthesis of specific protein. (©) Ribonucleic acid (RNA): It contains ribose sugar, bases from pyrimidine bases—uracil and cytosine, and two bases from purine base—adenine and guanine. A phosphate group is present at C-5 of the sugar unit, The repeating units, rbonucleotides, are linked by phosphate group. They are the polymers of ribonucleotide and have a single helix structure. RNA is associated with the process of learning and. memory storage, and helps in biosynthesis of protein. 15. Functions of Nucleic Acids: Two main functions of nucleic acids are: (@) Replication or heredity transfer: The double helix of DNA is the storehouse of the genetic information of the organism which is contained in the sequence of bases A, T, C, G on the strands of DNA. The process by which a DNA molecule produces two identical molecules of itself in the nucleus of the cell is called replication,() Protein synthesis: This is brought about in two steps: ( Transcription: Copying of sequence of bases from the DNA strand onto the RNA molecule is called transcription. During transcription, the double helix of the DNA partially unwinds and one of the two DNA strands serves as a template for the synthesis of RNA strand called messenger RNA (mRNA) which is complementary to a segment of the DNA chain. i) Translation: This isthe process in which mRNA directs protein synthesis in the cytoplasm of cell ‘with involvement of transfer RNA (RNA) and ribosomal particles (rRNA protein complexes). 16. (a) Codon: The sequence of nucleotides in mRNA molecules are read in a serial order in sets of three (triplet) at a time. Each triplet is called a codon. It specifies one amino acid. The mRNA codon recognises the amino acids through tRNAs which carry specific amino acids. (6) Gene: The sequence of hases or nucleotides in the DNA molecule which regulates the synthesis of a specific protein is called a gene. Every protein in the cell has a corresponding gene. The relationship, ‘between a nucleotide triplet (codon) and the amino acid is called genetic code. (©) Mutation: The chemical change in the sequence of bases in the DNA molecule can lead to synthesis of protein with an altered amino acid sequence is called mutation. This is brought ahout spontaneously by exposure to UV-rays, X-rays and chemicals. 17. Vitamins: Vitamins are generally regarded as organic compounds required in the diet in small amounts to perform specific biological functions for normal maintenance of optimum growth and health of the organism, Vitamins are classified into two groups depending upon their solubility in fat or water: ( Fat-soluble vitamins: Vitamins A, D, E and K are soluble in fat and oils but insoluble in water. They are stored in liver and adipose tissues. (Gi) Water-soluble vitamins: Vitamins belonging to group B and vitamin C are soluble in water. They must be supplied regularly in diet because they are readily excreted in urine and cannot be stored (except vitamin B ,) in our body Table 10.1: Some Important Vitamins, their Sources and their Deficiency Diseases Ese aieerettais __Sourees _Deticency Diseases Vitamin A | Fish iver ol, caus, buuter | Xerophihallia hardening of eomea of eye), aight Land mill blindness 2 | Vitamin By (Thiamine) | Yeas, milk, green | Beri-beri (loss of appetite, retarded growth) vegetables and cereals | 3. | Vitamin Bs (Riboflavin) | Milk, egg white, iver, | Cheilosis suring at corners of mouth and lips), kidney digestive disorders and burning sensation of the skin, 4, Vianin'B, (Pyridoxine) | Yeas mil, egg yolk, | Convulsions eee 5._ [Vitamin Br Dea fat eee end | Pema tend Cece cee) Vitamin C aa Sean Caiebic nn sear repens 7. | Viana D Saponies i mtg us | wacenr| (9g termite a ek fentegiyate aca thee ad i a & | Vitamin E ‘Vegelable oils like wheat | Increased fragility of RBCs and muscular weakness ‘germ oil, sunflower oil, etc. 9.__| Vitamin K Green leafy vegetables | Increased blood clotting time 18, Hormones: Hormones are molecules that act as intercellular messengers. These are produced by endocrine ‘lands in the body and are released directly in the blood stream. From here these are transported to the site of their action. Functions of hormones: (They help to maintain the balance of biological activities in the body. For example, insulin keeps the blood glucose level within the range, epinephrine and norepinephrine mediate response to external stimuli, growth hormones and sex hormones play role in growth and development.