Description : The disulphide bond is not broken under the usual conditions of (A) Filtration (B) Reduction (C) Oxidation (D) Denaturation
Last Answer : Answer : D
Description : In denaturation of proteins, the bond which is not broken: (A) Disulphide bond (B) Peptide bond (C) Hydrogen bond (D) Ionic bond
Last Answer : Answer : B
Description : The bond in proteins that is not broken under usual conditions of denaturation: (A) Hydrophobic bond (B) Hydrogen bond (C) Disulphide bond (D) Peptide bonds
Description : The bond in proteins that is not hydrolysed under usual conditions of denaturation: (A) Hydrophobic bond (B) Hydrogen bond (C) Disulphide bond (D) Peptide bonds
Last Answer : Answer : C
Description : A protein reacts with biuret reagent which indicates 2 or more (A) Blood clotting (B) Peptide bond (C) Disulphide bonds (D) Hydrophobic bonds
Description : Denaturation refers to the loss of the ______ structure of a ______ molecule. a. primary; carbohydrate b. molecular; fat c. secondary; starch d. tertiary; protein
Last Answer : d. tertiary; protein
Description : Denaturation of proteins results in (A) Disruption of primary structure (B) Breakdown of peptide bonds (C) Destruction of hydrogen bonds (D) Irreversible changes in the molecule
Description : In the insulin molecule, the number of intrachain disulphide bridges is (A) 1 (B) 2 (C) 3 (D) 4
Last Answer : Answer : A
Description : In the insulin molecule, the number of interchain disulphide brides is (A) 1 (B) 2 (C) 3 (D) 4
Description : Which of the following does not have disulphide bond? (A) Oxytocin (B) Vasopressin (C) Insulin (D) Glucagon
Description : Human growth hormone has (A) One polypeptide chain and one intra-chain disulphide bond (B) One polypeptide chain and two intra-chain disulphide bond (C) Two polypeptide chains joined by one disulphide bond (D) Two polypeptide chains joined by two disulphide bond
Description : An amino acid which contains a disulphide bond is (A) Lysine (B) Methionine (C) Homocysteine (D) Cystine
Description : A disulphide bond can be formed between (A) Two methionine residues (B) Two cysteine residues (C) A methionine and a cysteine residue (D) All of these
Description : In case of severe denaturation of protein, there is (A) Reversible denaturation (B) Moderate reversible denaturation (C) Irreversible denaturation (D) None of these
Description : Primary structure of a protein is formed by (A) Hydrogen bonds (B) Peptide bonds (C) Disulphide bonds (D) All of these
Description : Folding of newly synthesized proteins is accelerated by (A) Protein disulphide isomerase (B) Prolyl cis-trans isomerase (C) Chaperonins (D) All of these
Description : Tertiary structure of a protein describes (A) The order of amino acids (B) Location of disulphide bonds (C) Loop regions of proteins (D) The ways of protein folding
Description : What happens when a chemical bond is formed? (1) energy is always absorbed (2) energy in always released (3) more energy is released than is absorbed (4) energy is neither released nor ... as potential energy. Upon the breaking of these bonds the energy is released thereby creating usable energy.
Last Answer : Silver nitrate solution is kept in brown bottles in laboratory because - (1) it reacts with ordinary white bottles (2) brown bottles stops the passage of light through it (3) brown bottles do not react with it (4) brown bottles react with it
Description : How many ATP molecules could maximally be generated from one molecule of glucose, if the complete oxidation of one mole of glucose to CO2 and H2O yields 686 kcal and the useful chemical energy available in the high energy phosphate bond of one mole of ATP is 12 kcal? (a) 1 (b) 2 (c) 30 (d) 57
Last Answer : d) 57
Description : The two polypeptides of human insulin are linked together by (a) covalent bond (b) disulphide bridges (c) hydrogen bonds (d) phosphodiester bond.
Last Answer : (b) disulphide bridges
Description : 9.The reason behind the anti-parallel strand of DNA is 1. Hydrogen bond 2. Ionic bond 3. Phosphodiester bond 4. Disulphide bond
Last Answer : Ans: Phosphodiester bond.
Description : How does X-ray diffraction aid in the understanding of the structure of molecules?
Last Answer : X-ray diffraction is the investigative use of X-rays to discoverthe internal structure of a number of different things. The basicapproach is to set up a target material and direct a beam ... a broad field with diverging and complex investigativetechniques. Even so, the fundamentals remain the same.
Description : Electronic structure of a material is generally studied by (A) Metallurgical microscope (B) Electron diffraction (C) Spectroscopic techniques (D) X-ray
Last Answer : (C) Spectroscopic techniques
Description : Which one of the following techniques made it possible to genetically engineer living organisms? (a) Recombinant DNA techniques (b) X-ray diffraction (c) Heavier isotope labelling (d) Hybridization
Last Answer : (a) Recombinant DNA techniques
Description : X-ray diffraction can be observed by using __________. A. Diffraction Grating B. Rock salt crystal C. Convex lens D. Michelson’s interferometer
Last Answer : A. Diffraction Grating
Description : significant diffraction of X ray can be obtained A. By a single slit B. By a double slit C. By diffraction D. By Atomic crystal
Last Answer : A. By a single slit
Description : Denaturation of a protein is caused by (a) Heat (b) Acid (c) High salt concentration (d) All of the above
Last Answer : Ans:(d)
Description : Denaturation of a protein is caused by – (1) Heat (2) Acid (3) High salt concentration (4) All of the above
Last Answer : (4) All of the above Explanation: Denaturation of proteins involves the disruption and possible destruction of both the secondary and tertiary structures.
Description : Which of the following protein structures does “denaturation” destroy? (a) primary and secondary structures (b) secondary and tertiary structures (c) tertiary and quaternary structures (d) secondary, tertiary, and quaternary structures
Last Answer : secondary, tertiary, and quaternary structures
Description : What is the mode of action of autoclaving “Moist sterilisation”: A. Moist heat sterilization B. Protein denaturation
Last Answer : A. Moist heat sterilization
Description : RNA molecules can be broken up into three classes-which type of RNA molecule is translated into a protein sequence?
Last Answer : Messenger RNA (mRNA). mRNAs are the RNA transcripts that contain protein coding sequences which are translated into protein.
Description : Which of the following statement(s) is/are true concerning translation of the mRNA message to protein synthesis? a. An adaptor molecule, tRNA, recognizes specific nucleic acid bases and unites them ... and the free amino acid occurs in the free cytoplasm d. Complete protein synthesis takes hours
Last Answer : Answer: a, b The synthesis of protein involves conversion from a four-letter nucleotide language to one of 20 chemically distinct amino acids. This process is referred to as ... translation and be moving down the mRNA molecules simultaneously, thus increasing the rate of protein synthesis
Description : Agonists affect the receptor molecule in the following manner: A. Alter its amino acid sequence B. Denature the receptor protein C. Alter its folding or alignment of subunits D. Induce covalent bond formation
Last Answer : C. Alter its folding or alignment of subunits
Description : A light ray travelling from denser to rarer medium at an angle of incidence more than critical angle of concerned media pair suffers. (1) reflection (2) refraction (3) diffraction (4) total internal reflection
Last Answer : (4) total internal reflection Explanation: If the angle of incidence of light ray in the denser medium is greater than the critical angle of the concerned media pair, the light is not at all reflected in to the rarer medium but is totally reflected. This is known as 'total internal reflection'.
Last Answer : total internal reflection
Description : Denaturation of proteins involves breakdown of (A) Secondary structure(B) Tertiary structure (C) Quarternary structure(D) All of these
Description : The antigenic antibody functions of proteins by denaturation are frequently (A) Not changed (B) Changed (C) Both (A) and (B) (D) None of these
Description : During denaturation of proteins, all of the following are disrupted except (A) Primary structure (B) Secondary structure (C) Tertiary structure (D) Quaternary structure
Description : What are the usual agents that cause denaturation of proteins?
Last Answer : Brief heating, urea, X-ray, ultraviolet ray, high pressure, vigorous shaking.
Description : What are the features of denaturation?
Last Answer : Tungstic acid, phosphotungstic acid, trichloro acetic acid, picric acid, sulphosalicylic acid and tannic acid are protein precipitating agents.
Description : The number of ATP produced in the oxidation of 1 molecule of NADPH in oxidative phosphorylation is (A) Zero (B) 2 (C) 3 (D) 4
Description : Complete oxidation of one molecule of glucose into CO2 and H2O yields (A) 8 ATP equivalents (B) 15 ATP equivalents (C) 30 ATP equivalents (D) 38 ATP equivalents
Description : α-Oxidation i.e., the removal of one carbon at a time from the carboxyl end of the molecule has been detected in (A) Brain tissue (B) Liver (C) Adipose tissue (D) Intestine
Description : Oxidation of one molecule of glucose yields (A) 12 ATP (B) 24 ATP (C) 38 ATP (D) 38 ATP
Description : 1 molecule of palmitic acid on total oxidation to CO2 will yield molecules of ATP (as high energy bonds): (A) 129 (B) 154 (C) 83 (D) 25
Description : During complete oxidation, what is the net yield of ATP from one glucose molecule?
Last Answer : 38 ATP.
Description : This hormone has disulphide group: (A) Glucagon (B) Insulin (C) T4 (D) Epinephrine
Description : α-helix is stabilized by (A) Hydrogen bonds (B) Disulphide bonds (C) Salt bonds (D) Non-polar bonds
Description : Many globular proteins are stable in solution although they lack in (A) Hydrogen bonds (B) Salt bonds (C) Non-polar bonds (D) Disulphide bonds