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Biomolecules 14 Biomolecules 14.1 Carbohydrates 14.4 Vitamins 14.2 Proteins 14.5 Nucleic Acids 14.3 Enzymes Topicwise Analysis of Last 10 Years’ CBSE Board Questions 28 VSA SA I 24 SA II VBQ 20 LA 16 12 8 Number of questions of Number 4 0 14.1 14.2 14.3 14.4 14.5 Topic 8 Maximum total weightage is of Carbohydrates. 8 Maximum SA I and SA II type questions were asked from Carbohydrates and Vitamins 8 Maximum VSA type questions were asked from respectively. Carbohydrates. QUICK RECAP CARBOHYDRATES 8 General formula : Cx(H2O)y 8 Sugars or Saccharides : ey are optically active polyhydroxyaldehydes or ketones. 274 CBSE Chapterwise-Topicwise Chemistry 8 Classication : Carbohydrates are classied as either reducing or non-reducing sugars : Reducing sugars – Freealdehydic or ketonic group. – Reduce Fehling’ssolution and Tollens’ reagent. – e.g.,maltoseand lactose. Non-reducing sugars – Do nothavefreealdehydic or ketonicgroup – Do notreduce. Fehling’ssolutionand Tollens’ reagent. – e.g.,Sucrose. X On the basis of their behaviour towards hydrolysis : Carbohydrates Monosaccharides Oligosaccharides Polysaccharides Cannot behydrolysedfurther. Yield 2-10 monosaccharides Yield large number of (CH2 O)n where=n 3-7 on hydrolysis. monosaccharides on hydrolysis. ,glucose, fructose,ribose, etc. (C61HO05),n where=n 2-10 (C61HO05)wn here n = 100-3000 .s, ucrose, maltose, etc. .s, tarch, cellulose, etc. 8 Monosaccharides : X Glucose (C6H12O6) : An aldohexose as it contains six carbon atoms and aldehydic group. – Structure : Fischer projection of Haworth structure :s (Anomers) – Preparation : (Laboratory method) (Commercial method) Biomolecules 275 – Glucose was assigned open chain structure on the basis of following evidences : – Chemical reactions : : forms : X Fructose (C6H12O6) : A ketohexose as it contains six carbon atoms and ketonic group. – Structure : (Haworth Structures) 276 CBSE Chapterwise-Topicwise Chemistry X Mutarotation : e change in specic rotation of an optically active compound with time to an equilibrium value is called mutarotation. 8 Disaccharides and Polysaccharides Carbohydrate Hydrolysis Linkage Reducing property products Sucrose (Disaccharide) a-D-Glucose and C-1 (Glucose) and C-2(Fructose) Non-reducing b-D-Fructose Maltose (Disaccharide) a-D-Glucose C-1 (Glucose) and C-4 (glucose) Reducing Lactose (Disaccharide) b-D-Galactose and C-1 (Galactose) and C-4 (Glucose) Reducing b-D-Glucose Starch (Polysaccharide) Amylose and Amylose (C-1 and C-4 glycosidic Non-reducing amylopectin linkage betweeen a-D-Glucose) Amylopectin (C-1 and C-4 linkage between a-D-Glucose and branching occurs by C-1 and C-6 linkage) Cellulose (Polysaccharide) b-D-Glucose C-1(glucose) and C-4(glucose) Non-reducing Glycogen (Polysaccharide) a-D-Glucose C-1 (glucose) and C-4(glucose) Non-reducing PROTEINS 8 Proteins : ey are the biomolecules of the living system made up of nitrogenous organic compounds by condensation polymerisation of a-amino acids. 8 Classication of Amino Acids : Classication of amino acids Depending upon the relative number of amino ( NH2 ) and carboxyl ( COOH) groups On the basis of their synthesis Neutral Amino acids No.ofCOOHgroups=No.ofNH2 groups e.g.,Glycine, Alanine, Valine Essential Non-essential Acidic amino acids amino acids No.ofCOOHgroups>No.ofNH2 groups e.g.,Aspartic acid,Asparagine, Glutamic acid Cannot be synthesised Canbesynthesisedin in thebodyand must be thebody. Basic obtainedthrough diet. e.g.,glycine,alanine, No.ofNHg2 roups>No.ofCOOH e.g.,valine, leucine, lysine, glutamic acid,aspartic groups e.g.,Lysine, Arginine,Histidine isoleucine,arginine, etc. acid,etc. Biomolecules 277 8 Properties : X e products formed by the linking of amino X In aqueous solution, the carboxylic group can acids by peptide linkage are known as peptides. lose a proton and amino group can accept a X Peptides are further divided into di, tri, tetra proton giving rise to a dipolar ion known as depending upon the number of amino acids zwitter ion. is is neutral but contains both combined. positive and negative charges. X Oligopeptide : It contains anywhere between 2-10 amino acids. X Polypeptides : Structures with more than ten amino acids are known as polypeptides. X Since these form salts with acids as well as with bases, their chemical reactions are similar to primary amines and carboxylic acids. where R, R′, R′′ may be same or dierent. X A polypeptide with more than hundred amino acid residues, having molecular mass higher than 10,000 u is called a protein. 8 Classication of proteins : On the basis of molecular structure, proteins are classied as : X Isoelectric point : e pH at which dipolar Fibrous proteins ion (zwitter ion) exists as neutral ion, i.e., In Mbrous proteins, polypeptide chains areparallel +ve and –ve charge is equal and it does not andare heldtogetherbyhydrogenand disulphide migrate to either electrode, is called isoelectric bonds. eseareinsoluble in water, e.g.,keratinand point. e amino acids have least solubility in myosin. water at isoelectric point which helps in their separation. Globular proteins X Except glycine, all other naturally occurring Globular proteinsresults when thepolypeptide a-amino acids are optically active because they chains coil around to give three dimensional contain chiral, asymmetric carbon atom. sphericalshape.eseare solubleinwater,e.g., X ey exist in both D- and L-forms. Most insulin andalbumins. naturally occurring a-amino acids have 8 Structure : L-conguration. X Primary structure : It refers to the number and linear sequence of amino acids held together by peptide bonds. 8 Peptides and their classication : X Peptide bond : e bond formed between two amino acids by the elimination of a water molecule is called a peptide linkage or bond. X Secondary structure: It is due to folding or coiling of the peptide chain. It is mainly of two types : – a-helix : ese coils are stabilized by hydrogen bonds between carbonyl oxygen of rst amino acid to amide nitrogen of fourth amino acid. 278 CBSE Chapterwise-Topicwise Chemistry – b-pleated sheet structure : b-pleated sheet ENZYMES structure is formed when hydrogen bonds 8 e enzymes are biocatalysts produced by living are formed between the carbonyl oxygens cells which catalyse biochemical reactions and amide hydrogens of two or more in living organisms. Chemically, enzymes are adjacent polypeptide chains. e bonding in naturally occurring simple or conjugated proteins. b-pleated sheet structure is intermolecular Some enzymes may be non-proteins also. H-bonding. e structure is not planar HORMONES but is slightly pleated. Silk broin is rich in 8 Hormones : ey are the molecules that act as b-pleated sheets. intercellular messangers and are poured directly in the blood stream by endocrine glands. 8 Types of hormones : X Steroids : Estrogens and androgens X Polypeptides : Insulin and endorphins X Amino acid derivatives : Epinephrine and norepinephrine. X Tertiary structure : It represents overall folding VITAMINS of the polypeptide chains, i.e., further folding 8 Vitamins: ese are complex organic molecules of the secondary structure and the bonds which cannot be produced by the body and must responsible for such interaction are hydrophobic be supplied in small amounts in diet to carry out interactions, hydrogen bonds, ionic interactions, essential metabolic reactions which are required van der Waals’ forces and Disulphide bonds. for normal growth and maintenance of the body. X Quaternary structure : e spatial arrange-ment 8 Classication : of the subunits (two or more polypeptide chains) X Water soluble vitamins : Soluble in water. with respect to each other. Must be supplied regularly in diet as they are regularly excreted in urine (except vitamin B12) 8 Denaturation of proteins : e.g., Vitamin– B1, B2, B6, B12 and C. X When a protein in its native form, is subjected X Fat soluble vitamins : Soluble in fat and oils. Stored to physical changes like change in temperature in liver and adipose tissues e.g., Vitamin – A, D, or chemical changes like change in pH, the E and K. hydrogen bonds are disturbed. Due to this, globules unfold and helix get uncoiled and 8 Deciency of more than one vitamin in the protein loses its biological activity. is is called body causes avitaminosis while excess intake of denaturation of protein. vitamins (A and D) may cause hypervitaminoses. X e denaturation causes change in secondary NUCLEIC ACIDS and tertiary structures but primary structure 8 Nucleic acids are the polymers of nucleotides remains intact e.g., coagulation of egg white on present in nucleus of all living cells and play an boiling, curdling of milk, formation of cheese, important role in transmission of the hereditary when an acid is added to milk. characteristics and biosynthesis of proteins. Nucleotide 3– Pentose sugar Nitrogenous base Phosphategroup (PO4 ) Deoxyribose O Ribose –O PO– – Pyrimidine Purine O Uracil (U) Adenine (A) Thymine (T) Guanine (G) Cytosine (C) Biomolecules 279 8 Types of nucleic acids : H-bonds ( A T) and guanine (G) pairs with cytosine (C) through three H-bonds (G C). In case of RNA, adenine (A) pairs with uracil (U), (A U). 8 Replication : It is the process by which a single DNA molecule produces two identical copies of itself. 8 Protein synthesis : It occurs in two steps : X Transcription : It is the process of synthesis of 8 Charga’s rule : Amount of purine bases is always RNA. equal to that of pyrimidine bases. Purine base X Translation : e synthesis of proteins occur in of one strand of DNA molecule pairs with the cytoplasm of the cell. e m-RNA directs pyrimidine base of the other strand. Adenine protein synthesis with the help of r-RNA and (A) pairs with thymine (T) through two t-RNA. 280 CBSE Chapterwise-Topicwise Chemistry Previous Years’PREVIOUS CBSE YEARS Board MCQS Questions 14.1 Carbohydrates 17. Explain what is meant by the following : pyranose structure of glucose? VSA (1 mark) (AI, Foreign 2011) 1. Write the name of two monosaccharides 18. What is meant by ‘reducing sugars’? obtained on hydrolysis of lactose sugar.
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