Description : Bonds that are formed between two cysteine residues is (A) Disulphide (B) Peptide (C) Electrostatic (D) Hydrophobic
Last Answer : Answer : A
Description : An amino acid which contains a disulphide bond is (A) Lysine (B) Methionine (C) Homocysteine (D) Cystine
Last Answer : Answer : D
Description : Zinc finger motif is formed in some proteins by binding of zinc to (A) Two cysteine residues (B) Two histidine residues (C) Two arginine residues (D) Two cysteine and two histidine residues or two pairs of two cysteine residues each
Description : At the lowest energy level α-helix of polypeptide chain is stabilised (A) By hydrogen bonds formed between the H of peptide N and the carbonyl O of the residue (B) Disulphide bonds (C) Non polar bonds (D) Ester bonds
Description : In E. coli the chain initiating amino acid in protein synthesis is (A) N-formyl methionine(B) Methionine (C) Serine (D) Cysteine
Description : Cysteine can partially meet the requirement of (A) Phenylalanine (B) Threonine (C) Methionine (D) None of these
Last Answer : Answer : C
Description : Sulphydryl group is present in (A) Cysteine (B) Methionine (C) Both (A) and (B) (D) None of these
Description : Cystine is synthesized from (A) Cysteine (B) Methionine (C) Arginine (D) Leucine
Description : The limiting amino acid in wheat is (A) Leucine (B) Lysine (C) Cysteine (D) Methionine
Last Answer : Answer : B
Description : Methionine is synthesized in human body from (A) Cysteine and homoserine (B) Homocysteine and serine (C) Cysteine and serine (D) None of these
Description : Cysteine can be synthesized from methionine and (A) Serine (B) Homoserine (C) Homocysteine (D) Threonine
Description : In humans the sulphur of methionine and cysteine is excreted mainly as (A) Ethereal sulphate (B) Inorganic sulphate (C) Sulphites (D) Thioorganic compound
Description : All the following are sulphur containing amino acids found in proteins except (A) Cysteine (B) Cystine (C) Methionine (D) Threonine
Last Answer : (D) Threonine
Description : Ultraviolet light can damage a DNA strand causing (A) Two adjacent purine residue to form a covalently bounded dimer (B) Two adjacent pyrimidine residues to form covalently bonded dimer (C) Disruption of phosphodiesterase linkage (D) Disruption of non-covalent linkage
Description : The amino terminal of all polypeptide chain at the time of synthesis in E. coli is tagged to the amino acid residue: (A) Methionine (B) Serine (C) N-formyl methinine(D) N-formal serine
Description : For the synthesis of amino acids cysteine, cystine and methionine the element required is a. Sulphur b. Oxygen c. Nitrogen d. None of these
Last Answer : Ans: D
Description : Toxicity of mercury and cadmium is being reversed by protein mainly using the amino acid residue ____________. (a) Cysteine (b) Glycine (c) Lewcine (d) Lysine
Last Answer : (a) Cysteine
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 : Which of the following does not have disulphide bond? (A) Oxytocin (B) Vasopressin (C) Insulin (D) Glucagon
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 : In denaturation of proteins, the bond which is not broken: (A) Disulphide bond (B) Peptide bond (C) Hydrogen bond (D) Ionic bond
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 disulphide bond is not broken under the usual conditions of (A) Filtration (B) Reduction (C) Oxidation (D) Denaturation
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
Description : In a protein molecule the disulphide bond is not broken by (A) Reduction (B) Oxidation (C) Denaturation (D) X-ray diffraction
Description : α-Helix is formed by (A) Hydrogen bonds (B) Hydrophobic bonds (C) Electrostatic bonds (D) Disulphide bonds
Description : Primary structure of a protein is formed by (A) Hydrogen bonds (B) Peptide bonds (C) Disulphide bonds (D) All of these
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 : The covalent bond that is repeatedly present between different amino acid residues in a protein is called (a) p-bond (b) hydrogen bond (c) peptide bond (d) metallic bond
Last Answer : Ans:(c)
Description : The number of intra-chain disulphide bonds in pro-insulin: (A) One (B) Two (C) Three (D) Four
Description : This hormone has disulphide group: (A) Glucagon (B) Insulin (C) T4 (D) Epinephrine
Description : In the insulin molecule, the number of intrachain disulphide bridges is (A) 1 (B) 2 (C) 3 (D) 4
Description : In the insulin molecule, the number of interchain disulphide brides is (A) 1 (B) 2 (C) 3 (D) 4
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
Description : Proteins react with biuret reagent which is suggestive of 2 or more (A) Hydrogen bonds (B) Peptide bonds (C) Disulphide bonds (D) Hydrophobic bonds
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 : In quaternary structure, subunits are linked by (A) Peptide bonds (B) Disulphide bonds (C) Covalent bonds (D) Non-covalent bonds
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 : The a-helix of proteins is (A) A pleated structure (B) Made periodic by disulphide bridges (C) A non-periodic structure (D) Stabilised by hydrogen bonds between NH and CO groups of the main chain
Description : Many globular proteins are stable in solution inspite they lack in (A) Disulphide bonds (B) Hydrogen bonds (C) Salt bonds (D) Non polar bonds
Description : Buffering action of haemoglobin is mainly due to its (A) Glutamine residues (B) Arginine residues (C) Histidine residues (D) Lysine residues
Description : Blue print for genetic information residues in (A) mRNA (B) tRNA (C) rRNA (D) DNA
Description : Glycoproteins are marked for destruction by removal of their (A) Oligosaccharide prosthetic group (B) Sialic acid residues (C) Mannose residues (D) N-terminal amino acids
Description : Leucine zipper motif is seen in some helical proteins when leucine residues appear at every (A) 3rd position (B) 5th position (C) 7th position (D) 9th position
Description : Number of guanine and cytosine residues is equal in (A) mRNA (B) tRNA (C) DNA (D) None of these
Description : Number of amino acid residues in glucagons is (A) 29 (B) 34 (C) 51 (D) 84
Description : Amino acid residues which are essential for the biological activity of PTH are (A) N-terminal 34 amino acids (B) N-terminal 50 amino acids (C) C-terminal 34 amino acids (D) C-terminal 50 amino acids