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Nehru Arts Science and College Reaccredited with “A” Grade by NAAC ISO 9001 : 2008 & 14001:2004 Certified Recognised by UGC & Affiliated to Bharathiar University DEPARTMENT OF MICROBIOLOGY SEMESTER III : PAPER BIOCHEMISTRY I QUESTION BANK Saranya Rathan NEHRU ARTS AND SCIENCE COLLEGE DEPARTMENT OF MICROBIOLOGY Question Bank CLASS : II B.Sc. SUBJECT TITLE: ALLIED BIOCHEMISTRY I _________________________________________________________________________ UNIT-I Carbohydrates: Monosaccharides - Definition, classification, structure and properties. Disaccharides Definition, types, structure and biological importance. Polysaccharides-types and properties. UNIT-II Lipids - Definition, Classification and properties of lipids. Types of fatty acids -saturated, unsaturated and essential fatty acids. Classification and significance of lipoproteins and phospholipids. Importance of steroids, structure and biological significance of cholesterol. UNIT-III Amino acids: Classification of amino acids, essential amino acids, reactions of amino and carboxyl groups of amino acids. Proteins: Definition, classification and function of Proteins, structural levels of organization (Preliminary treatment). Denaturation and isoelectric point of proteins. UNIT-IV Nucleic acids: Components of DNA and RNA. Double helical structure of DNA. Structure and types of RNA. Denaturation and renaturation of DNA. Genetic code. Protein synthesis (an outline) UNIT-V Enzymes: Classification of enzymes with examples, coenzymes and cofactors (structures not needed). Active site: Lock and Key model, Induced fit hypothesis. Factors affecting enzyme activity. Types of inhibition of enzyme action. Chemical and industrial applications of enzymes. Test Books: 1. Fundamentals of biochemistry – A.C. Deb New Central Book Agency, Calcutta 6th Edition. Reference Books: 1. Biochemistry – Lehninger, Nelson, Cox-CBS Publishers 2. Harper’s Biochemistry: R.K. Murray, D.K Granner, P.A. Mayes and U.W.Rodwell –Lange Medical publications, 23rd edition. 3. Textbook of Medical Biochemistry – Rana Shindae and Chatterjee. UNIT – I Part A 1. The general formula of Monosaccharides is (1) CnH2nOn (2) C2nH2On (3) CnH2O2n (4) CnH2nO2n 2. A pentose sugar is (1) Dihydroxyacetone (2) Ribose (3) Erythrose (4)Glucose 3. Sucrose consists of (1) Glucose + glucose (2) Glucose + fructose (3) Glucose + galactose (4) Glucose + mannose 4. The number of isomers of glucose is (1) 2 (2) 4 (3) 8 (4) 16 5. A keto sugar is (1) Fructose (2) Ribose (3) Erythrose (4) Glucose 6. Starch consists of (1) Polymer of Glucose (2) Polymer of Glucose + fructose(3) Polymer of Glucose and galactose (4) Monomer of Glucose 7. The general test for detection of carbohydrates is________ (1) Iodine test (2) Molisch test (3) Barfoed test (4)Osazone test 8. ____________ is a polysaccharide and it is component of cell walls in plants. (1) Cellulose (2) starch (3) glycogen (4) glucose 9. The substance _______________ is known as animal starch. (1) Glucose (2) starch (3) glycogen (4) chitin 10. Starch is a (1) Homopolysaccharide (2) Monosaccharide (3)Disaccharide (4) Heteropolysaccharid 11. The most important epimer of glucose is (1) Galactose (2) Fructose (3) Arabinose (4) Xylose. 12. The carbon atom present in pentose sugar is _____ carbons (1) 5 (2) 3 (3) 6 (4) 4 13. All of the following are storage carbohydrates except (1) Starch (2) Glycogen (3) Amylopectin (4) Cellulose 14. Which of the following is a polysaccharide found in human muscle cells? (1) Myoglobin (2) Collagen (3) Glycogen (4) Amylose 15. Compounds having the same structural formula but differing in spatial configuration are known as (1) Stereoisomers (2) Anomers (3) Optical isomers (4)Epimers 16. Which of the following is a non-reducing sugar? (1) Isomaltose (2) Maltose (3) Lactose (4) sucrose 17. Lactose consists of (1) Glucose + glucose (2) Glucose + fructose (3) Glucose + galactose (4) Glucose + mannose. 18. Maltose consists of (1) Glucose + glucose (2) Glucose + fructose (3) Glucose + galactose (4) Glucose + mannose 19. The polysaccharide found in the exoskeleton of invertebrates is (1) Pectin (2) Chitin (3) Cellulose (4) Chondroitin sulphate 20. The most abundant carbohydrate found in nature is (1) Starch (2) Glycogen (3) Cellulose (4) Chitin 21. Iodine gives a blue colour with (1) Starch (2) Glycogen (3) Cellulose (4) Chitin 22. Amylose is a constituent of (1) Starch (2) Glycogen (3) Cellulose (4) Chitin 23. A aldotriose sugar is (1) Glyceraldehyde (2) Ribose (3) Erythrose (4) Fructose 24. Which of the following is a reducing sugar? (1) glucose (2) fructose (3) Maltose (4) All 25. A carbohydrate, commonly known as dextrose is (1) Dextrin (2) D-Fructose (3) D-Glucose (4) Glycogen Part – B 1. Define Carbohydrates and explain their classification with examples. 2. Explain briefly about the properties of Disaccharides 3. Explain about the structure and properties of Monosaccharide’s. 4. Briefly note on structural polysaccharides. 5. Discuss on three hetero polysaccharides with its structure. Part C 1. Explain in detail about the types of disaccharides, structure and their biological importance. 2. Explain in detail about Polysaccharides-types and properties. 3. Define Carbohydrates? How they are classified? Briefly write on sub classification of Monosaccharides with example. 4. Describe the disaccharide with suitable example along with its structural illustrations. 5. Briefly note on storage polysaccharides. 6. Explain structure and function of starch and cellulose UNIT II Part A 1. Esters of fatty acids with glycerols is (1) Fats (2) Waxes (3) Lipids (4) None of the above 2. In mammals, the major fat in adipose tissues is (1) phospholipds (2) cholesterol (3) Sphingolipids (4)Triacylglycerol 3. Which is derived lipid (1) Triglycerides (2) cholesterol (3) beeswax (4)kerosene 4. The fatty acid containing one or more double bond is called as (1) Unsaturated fatty acid (2) Saturated fatty acid (3)Essential fatty acid (4) none of the above 5. Essential fatty acid are (1) Linoleic acid (2) Linolenic acid (3) Arachidonic acid (4)All these 6. Lipids are stored in the body mainly in the form of (1) Phospholipids (2) Glycolipids (3) Triglycerides (4)Fatty acids 7. The fatty acid with no bond is called as (1) Saturated fatty acid (2) Unsaturated fatty acid (3)Essential fatty acid (4) none of the above 8. A fatty acid which is not synthesized in human body and has to be supplied in the diet is (1) Palmitic acid (2) Oleic acid (3) Linoleic acid (4)Stearic acid 9. An example of a saturated fatty acid is (1) Palmitic acid (2) Oleic acid (3) Linoleic acid (4) Erucic acid 10. Higher alcohol present in waxes is (1) Benzyl (2) methyl (3) ethyl (4) cetyl 11. The highest phospholipids content is found in (1) chylomicrons (2) VLDL (3) LDL (4) HDL 12. The major lipid in chylomicrons is (1) Triglycerides (2) Phospholipids (3) Cholesterol (4)Free fatty acids 13. Number of carbon atoms in cholesterol is (1) 17 (2) 19 (3) 27 (4) 30 14. The nitrogenous base in lecithin is (1) Ethanolamine (2) Choline (3) Serine (4) Betaine 15. Elevated plasma level of the following projects against atherosclerosis: (1) Chylomicron (2) VLDL (3) LDL (4) HDL 16. Very low density lipoproteins are also known as (1) Beta-lipoproteins (2) Pre Beta—lipoproteins (3)alpha-lipoproteins (4) None of these 17. low density lipoproteins are also known as (1) Beta-lipoproteins (2) Pre Beta—lipoproteins (3) alpha-lipoproteins (4) None of these 18. Cholesterol is a (1) Animal sterol (2) M.F. C27 H46O (3) 5 methyl groups(4) All of these 19. Biological functions of lipids include (1) Source of energy (2) Insulating material (3)Maintenance of cellular integrity (4) All of these 20. Cephalins are composed of (1) Glycerol + Fatty acids + Phosphoric acid + Choline (2)Glycerol + Fatty acids + Phosphoric acid + Ethanolamine (3) Glycerol + Fatty acids + Phosphoric acid + Serine (4) Glycerol + Fatty acids + Phosphoric acid + Beaine 21. Phospholipids are important cell membrane components since (1) They have glycerol (2) Form bilayers in water (3) Have polar and non-polar portions (4) Combine covalently with proteins 22. The lipoprotein with the fastest electrophoretic mobility and lowest TG content are (1) VLDL (2) LDL (3) HDL (4) Chylomicrones 23. The compound which has the lowest density is (1) Beta-lipoproteins (2) Pre Beta—lipoproteins (3) alpha-lipoproteins (4) Chylomicrone 24. The density of lipoproteins increases as the protein content (1) Increases (2) decreases (3) Highly decreases (4)Slightly and promptly decrease 25. Which of the following is a polyunsaturated fatty acid? (1) Palmitic acid (2) Palmitoleic acid (3) Linoleic acid (4)Oleic acid Part B 1. What are derived lipids? Give some examples. 2. Write a briefly note on steroids. 3. Define phospholipids and write the properties. 4. Explain briefly about Compound lipids and its properties. 5. Briefly explain the properties of lipids? 6. Write in a brief note about cholesterol. 7. Discuss the biological significance of phospholipids. 8. Bring out the structure and biological significance of cholesterol. Part C 1. How are lipids classified? Briefly explain each group 2. Explain structure and function of starch and cellulose 3. Explain the classification of lipoproteins? Explain structure and functions of any two disaccharides. 4. Explain about the classification of lipids in detail. 5. Explain in detail on types and properties of fatty acids. Unit III Part A 1. Sulphur containing amino acid is (1) Methionine (2) Leucine (3) Valine (4) Asparagine 2. The chief protein of cow’s milk is (1) Albumin (2) Vitellin (3) Livetin (4) Casein 3. The protein present in nail is (1) Keratin (2) Elastin (3) Collagen (4) Myosin 4. Egg contains (1) Protein (2) fat (3) Carbohydrates (4) calcium 5. Non essential amino acids_______ (1) are not components of tissue proteins (2) Synthesized in the body from essential amino acids (3) Should be supplemented in diet (4) May be synthesized in the body in diseased states 6. Primary structure of a protein is formed by (1) Hydrogen bonds (2) Peptide bonds (3) Disulphide bonds (4) All of these 7. Transfer of amino group from one aminoacid to other aminoacid is called as (1) transamination (2) deamination (3) transaminidation(4) transamidation 8. Removal of amino group from one aminoacid is called as (1) transamination (2) deamination (3) transaminidation(4) transamidation 9. Removal of carboxyl group from an aminoacid is called as (1) transamination (2) deamination (3) decarboxylation(4) transamidation 10. Proteins are (1) monomer of aminoacid (2) polymer of aminoacid (3)madeup of amino group and carboxyl group (4) madeup of amino group alone 11. All proteins contain the (1) Same 20 amino acids (2) Different amino acids (3)300 Amino acids occurring in nature (4) Only a few amino acids 12. An aromatic amino acid is (1) Lysine (2) Tyrosine (3) Leucine (4) Arginine 13. An amino acid not found in proteins is (1) Alanine (2) Proline (3) Lysine (4) Histidine 14. A disulphide bond can be formed between (1) Two methionine residues (2) Two cysteine residues (3)methionine and a cysteine residue (4) All of these 15. A Zwitterion is (1) Positive ion (2) Negative ion (3) Both (a) and (b) (4)None of these 16. Which among the following is a basic amino acid? (1) Aspargine (2) Arginine (3) Proline (4) Alanine 17. The useful reagent for detection of amino acids is (1) Molisch reagent (2) Dichlorophenol Indophenol (3)Ninhydrin (4) Biuret 18. Denaturation of proteins leads to loss of biological activity by (1) formation of amino acid (2) loss of primary structure(3) loss of both primary and secondary structure (4) loss of secondary and tertiary structure 19. Casein, the milk protein is (1) Nucleoprotein (2) Chromoprotein (3) Phosphoprotein(4) Glycoprotein 20. In proteins the ?-helix and ?-pleated sheet are examples of (1) Primary structure (2) Secondary structure (3) Tertiary structure (4) Quaternary structure 21. Glutelins are present in (1) Milk (2) Meat (3) Eggs (4) Cereals 22. The most abundant protein in mammals is (1) Albumin (2) Haemoglobin (3) Collagen (4) Elastin 23. The amino acid which contains an indole group is (1) Histidine (2) Arginine (3) Glycine (4) Tryptophan 24. One of the following has a phenolic group: (1) Histidine (2) Hydroxy lysine (3) Seratonine (4)Hydroxy proline 25. The major end product of protein nitrogen metabolism in man is (1) Glycine (2) Uric acid (3) Urea (4) NH3 Part B 1. Define iso electric point and briefly explain about it. 2. Differentiate essential amino acid from nonessential amino acid. 3. Write a note on protein classification. 4. Give an account protein denaturation. 5. Enlist the reactions carried out by functional group of aminoacids. 6. Write a note on denaturation of proteins and agents responsible for denaturation. Part C 1. Give an account on classification of aminoacids. 2. Describe the structural level of proteins with suitable diagram. 3. Explain in detail about classification of amino acids based on side chain. 4. Give in detail about the nutritional and functional classification of aminoacids with example. 5. Illustrate the reactions of amino and carboxyl groups of amino acids. UNIT IV Part A 1. The amount of adenine is always equal to the amount of ____ in DNA. (1) Cytosine (2) uracil (3) guanine (4) thymine 2. The nucleotide consists of (1) Purine + sugar + phosphorous (2) Purine or pyrimidine base + sugar + phosphorous (3) Purine or pyrimidine base + sugar (4) Purine or pyrimidine base + phosphorous 3. The nucleoside consists of (1) sugar + phosphorous (2) Purine + pyrimidine base + sugar + phosphorous (3) Purine or pyrimidine base + sugar (4) Purine or pyrimidine base + phosphorous 4. The sugar found in DNA is (1) Xylose (2) Ribose (3) Deoxyribose (4) Ribulose 5. RNA does not contain (1) Uracil (2) Adenine (3) Thymine (4) Ribose 6. The sugar moiety present in RNA is (1) Ribulose (2) Arabinose (3) Ribose (4) Deoxyribose 7. The structure of tRNA appears like a (1) Hair pin (2) Helix (3) clover leaf (4) Coil 8. DNA was discovered by (1) Meischer (2) Watson and Crick (3) Griffith (4) Avery 9. The nucleotide present only in RNA is _______ (1) Cytosine (2) Uracil (3) Guanine (4) Thymine 10. The structure of DNA is (1) double strand (2) single strand (3) double stranded helical (4) single stranded helical 11. DNA rich in G-C pairs have (1) 1 (2) 2 (3) 3 (4) 4 12. DNA rich in A-T pairs have (1) 1 (2) 2 (3) 3 (4) 4 13. The bond between the nucleotide is ______ (1) Hydrogen bond (2) Phosphodiester Bond (3)Phosphate bond (4) covalent bond 14. The nitrogenous bases will be attached to the sugar moiety at the position of ______ (1) 1 (2) 5 (3) 3 (4) 2 15. Difference between the DNA and RNA is ______ (1) Sugar (2) nitrogenous base (3) Both (4) None 16. In DNA 2 strands will be______conformation (1) parallel (2) antiparallel (3) Same (4) opposite 17. Degeneracy of the genetic code means that (1) a given base triplet can code for more than one amino acid (2) there is no punctuation in the code sequence (3)the third base in a codon is net important for coding (4) a given amino acid can be coded for by more than one base triplet 18. A purine nucleotide is (1) AMP (2) UMP (3) CMP (4) TMP 19. A pyrimidine nucleotide is (1) GMP (2) CMP (3) AMP (4) IMP 20. Translation refers to (1) DNA replication (2) protein synthesis using mRNA and tRNA (3) mRNA synthesis from DNA (4) converting an inactive protein into its active form 21. Which of the following molecules has an amino acid attached to it? (1) DNA (2) tRNA (3) mRNA (4) all of the above 22. A codon is (1) one three-letter “word” in the genetic code (2) a protein cap on the end of a chromosome. (3) the enzyme that makes DNA replication possible. (4) a special kind of RNA that provides energy for cell fission. 23. Genetic code is having all the properties except (1) universal (2) comma less (3) overlapping (4)ambegious 24. Start codon is (1) UAA (2) AUG (3) UAG (4) UGA 25. Stop codon is (1) UAA (2) all the three (3) UAG (4) UGA Part B 1. Describe the structure and types of RNA. 2. DNA is double helical structure in nature - justify. 3. Illustrate the chemistry of DNA molecule 4. Give an account on genetic code and its properties. 5. Write about the components of DNA with structures. 6. Write about the component of RNA. Part C 1. DNA is double helical structure in nature - justify. 2. Give an account on genetic code and its properties 3. llustrate the structure and types and RNA. 4. Explain in detail about the synthesis of protein. 5. Write in detail about the Nucleic acids. 6. Define – nucleotide and nucleoside and explain in detail. 7. Illustrate the structure of ribosome and its function in detail. UNIT V Part A 1. The enzyme found in the tears is (1) Lysozyme (2) Protease (3) Trypsin (4) Peptidase 2. Ribozymes are (1) Enzymes which combine the ribosomal subunits (2)Enzymes which dissociate (3) Enzymes made up of RNA(4) Enzymes present in ribosomes 3. Coenzymes are (1) Heat stable, dialyzable, non protein organic molecules (2) Soluble, colloidal, protein molecules (3)Structural analogue of enzymes (4) Different forms of enzymes 4. Factors affecting enzyme activity is (1) Concentration (2) pH (3) Temperature (4) All of these 5. The enzyme found in the saliva is (1) Lysozyme (2) Protease (3) Amylase (4) Lipase 6. Two amino acids of the standard 20 contain sulfur atoms. They are: (1) cysteine and serine (2) cysteine and threonine (3)methionine and cysteine (4) Methionine and serine 7. Enzymes, which are produced in inactive form in the living cells, are called (1) Papain (2) Lysozymes (3) Apoenzymes (4)Proenzymes 8. Fischer’s ‘lock and key’ model of the enzyme action implies that (1) The active site is complementary in shape to that of substance only after interaction. (2) The active site is complementary in shape to that of substance (3)Substrates change conformation prior to active site interaction (4) The active site is flexible and adjusts to substrate 9. In enzyme kinetics Vmax reflects (1) The amount of an active enzyme (2) Substrate concentration (3) Half the substrate concentration (4)Enzyme substrate complex 10. An example of enzyme inhibition is (1) Reversible inhibition (2) Irreversible inhibition (3)Allosteric inhibition (4) All of these 11. Which is true about enzymes, (1) they always increase rate of reaction (2) they always decrease rate of reaction (3) they do not disturb the equilibrium (4) Always carry irreversible reactions 12. Blocking action of enzyme through blocking its active site is (1) Allosteric inhibition (2) Feedback inhibition (3)Competitive inhibition (4) Noncompetitive inhibition 13. Blocking action of enzyme through blocking other than active site is (1) Allosteric inhibition (2) Feedback inhibition (3)Competitive inhibition (4) Noncompetitive inhibition 14. An example of ligases is (1) Succinate thiokinase (2) Alanine racemase (3)Fumarase (4) Aldolase 15. An example of lyases is (1) Glutamine synthetase (2) Fumarase (3) Cholinesterase(4) Amylase 16. The kinetic effect of purely competitive inhibitor of an enzyme (1) Increases Km without affecting Vmax (2) Decreases Km without affecting Vmax (3) Increases Vmax without affecting Km (4) Decreases Vmax without affecting Km 17. In reversible non-competitive enzyme activity inhibition (1) Vmax is increased (2) Km is increased (3) Km is decreased (4) Concentration of active enzyme is reduced 18. The induced fit model of enzyme action was proposed by (1) Fischer (2) Koshland (3) Mitchell (4) Markert 19. Competitive inhibition can be relieved by raising the (1) Enzyme concentration (2) Substrate concentration(3) Inhibitor concentration (4) None of these 20. An enzyme is a (1) Carbohydrate (2) Lipid (3) Protein (4) Nucleic acid 21. In normal resting state of human most of the blood glucose burnt as fuel is consumed by (1) Liver (2) Brain (3) Adipose tissue (4) Muscles 22. Feedback inhibition of enzyme is influenced by (1) Enzyme (2) External factors (3) End product (4)Substrate 23. Characteristic features of active site are (1) Flexible in nature (2) Site of binding (3) Acidic (4) Both (a) and (b) 24. The enzyme used in baby foods preparation is__________ (1) Lysozyme (2) Protease (3) Trypsin (4) Peptidase 25. Enzyme involved in joining together two substrates is (1) ligase (2) Hydrolase (3) Lyase (4) Transferase Part B 1. Define active site? Explain the models proposed for binding of substrate with enzyme. 2. Explain about Lock and key model. 3. Explain in detail about induced fit model. 4. Give any 5 Chemical and industrial applications of enzymes. 5. Explain about the cofactor 6. Explain brief about the coenzymes. Part C 1. Analyze the factors affective enzyme activity. 2. Explain about the mechanism of enzyme inhibition and inhibitors. 3. Give an account on classification of enzymes with example. 4. Write in detail about the factors affecting enzyme activity. 5. Write in detail about the types of inhibition of enzyme action.