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
Last Answer : Answer : A
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
Last Answer : Answer : D
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
Last Answer : Answer : B
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 : In quaternary structure, subunits are linked by (A) Peptide bonds (B) Disulphide bonds (C) Covalent bonds (D) Non-covalent bonds
Description : Bonds that are formed between two cysteine residues is (A) Disulphide (B) Peptide (C) Electrostatic (D) Hydrophobic
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 : 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 : Which bond is present in the primary structure of protein? (A) Ester (B) Hydrogen (C) Ionic bond (D) Peptide
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 : α-Helix is formed by (A) Hydrogen bonds (B) Hydrophobic bonds (C) Electrostatic bonds (D) Disulphide 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 hydrogen bonds between peptide linkages of a protein molecules are interfered by (A) Guanidine (B) Uric acid (C) Oxalic acid (D) Salicylic acid
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 : 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 : The double helical structure of DNA is held together by (a) sulfur-sulfur linkages (b) peptide bonding (c) hydrogen bonding (d) glycosidic bonds
Last Answer : hydrogen bonding
Description : The chemical forces that bind most coenzymes and substrates to enzymes such as LDH are (A) Hydrogen bonds (B) Peptide bonds (C) Coordinate bonds (D) Covalent bonds
Description : The hydrogen bonds between peptide linkages are interfered by (A) Guanidine (B) Uric acid (C) Salicylic acid (D) Oxalic acid
Description : The formation of a peptide bond during the elongation step of protein synthesis results in the splitting of how many high energy bonds? (A) 1 (B) 2 (C) 3 (D) 4
Description : Edman’s reaction can be used to (A) Determine the number of tyrosine residues in a protein (B) Determine the number of aromatic amino acid residues in a protein (C) Determine the amino acid sequence of a protein (D) Hydrolyse the peptide bonds in a protein
Description : A coiled structure in which peptide bonds are folded in regular manner by (A) Globular proteins (B) Fibrous proteins (C) Both (A) and (B) (D) None of these
Description : Which bonds are the last to break when an enzyme is heated 1 disulphide 2 hydrogen 3 hydrophobic interactions 4 ionic?
Last Answer : ionic
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 : The only correct statement about chymotrypsin is (A) It is formed from trypsin (B) Carboxypeptidase converts trypsin into chymotrypsin (C) Its optimum pH is around 7 (D) It hydrolyses peptide bonds involving basic amino acids
Description : All the following statements about pepsin are correct except (A) It is smaller than pepsinogen (B) It is formed by the action of HCl on its precursor (C) Its optimum pH is 1.0–2.0 (D) It hydrolyses the C-terminal and N-terminal peptide bonds of proteins
Description : Which of the following is the first step in the determination of the primary structure of proteins? (a) determining the number and kind of amino acids in the peptide (b) reducing the disulfide bridges ... (c) protecting the N-terminal of the peptide (d) protecting the C-terminal of the peptide
Last Answer : reducing the disulfide bridges in the protein
Description : The number of intra-chain disulphide bonds in pro-insulin: (A) One (B) Two (C) Three (D) Four
Description : The two strands of the DNA double helix are held together by (a) Hydrogen bonds (b)C=C double bonds (c) Hydrophobic bonds (d) Peptide bonds
Last Answer : Ans:(a)
Description : Which of the following statements is not correct? (a) In man insulin is synthesised as a proinsulin. (b) The proinsulin has an extra peptide called C-peptide. (c) The functional insulin has A and B chains linked together by hydrogen bonds. (d) Genetically engineered insulin is produced in E.Coli.
Last Answer : (c) The functional insulin has A and B chains linked together by hydrogen bonds.
Description : When all the peptide bonds of a protein have been broken down . The result would be
Last Answer : When all the peptide bonds of a protein have been broken down . The result would be A. Amide B. Oligosaccharide C. Polypeptide D. Amino acid
Description : Anhydro bonds of protein are called (a) Glycosidic (b) Peptide (c) Easter (d) Diester.
Last Answer : (b) Peptide
Description : How peptide bonds are formed? -Biology
Last Answer : answer:
Description : Ninhydrin reaction gives a purple colour and evolves CO2 with (A) Peptide bonds (B) Histamine (C) Ergothioneine (D) Aspargine
Description : Chymotrypsin is specific for peptide bonds containing (A) Uncharged amino acid residues (B) Acidic amino acids (C) Basic amino acid (D) Small amino acid residues
Description : The enzyme trypsin is specific for peptide bonds of (A) Basic amino acids (B) Acidic amino acids (C) Aromatic amino acids (D) Next to small amino acid residues
Description : How many peptide bonds are present in a trip- eptide?
Last Answer : A tripeptide is a combination of three amino ac- ids; so there are two peptide 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 a protein molecule the disulphide bond is not broken by (A) Reduction (B) Oxidation (C) Denaturation (D) X-ray diffraction
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 : 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 : The hydrogen bonds in the secondary and tertiary structure of proteins are directly attacked by (A) Salts (B) Alkalies (C) Detergents (D) All of these
Description : Which of the following is the quaternary structure of proteins concerned with? (a) sequence of amino acids in the peptide chain (b) description of the way the peptide chains are arranged with ... (c) location of the disulfide bridges in the peptide chain (d) conformation of the protein backbone
Last Answer : description of the way the peptide chains are arranged with respect to each other
Description : In DNA, three hydrogen bonds are formed between (A) Adenine and guanine (B) Adenine and thymine (C) Guanine and cytosine (D) Thymine and cytosine
Description : Hydrophobic bonds are formed in protein be- tween which amino acids?
Last Answer : Valine, leucine and isoleucine residues.
Description : Which of the following statement about the peptide bond is true? (A) It is a carbon-carbon bond (B) It has cis hydrogen and oxygen groups (C) It is planar (D) It has rotational freedom
Description : Intrinsic factor is chemically a (A) Protein (B) Glycoprotein (C) Mucopolysaccaride (D) Peptide
Description : Which method of protein estimation is depen- dent on the intact peptide bond?
Last Answer : Biuret method.
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.