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 broken under usual conditions of denaturation: (A) Hydrophobic bond (B) Hydrogen bond (C) Disulphide bond (D) Peptide bonds
Last Answer : Answer : D
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 : Bonds that are formed between two cysteine residues is (A) Disulphide (B) Peptide (C) Electrostatic (D) Hydrophobic
Last Answer : Answer : A
Description : Primary structure of a protein is formed by (A) Hydrogen bonds (B) Peptide bonds (C) Disulphide bonds (D) All of these
Description : α-Helix is formed by (A) Hydrogen bonds (B) Hydrophobic bonds (C) Electrostatic bonds (D) Disulphide bonds
Description : Group that reacts in the Biuret test: (A) Peptide (B) Amino group (C) Carboxylic group (D) Aldehyde group
Description : In quaternary structure, subunits are linked by (A) Peptide bonds (B) Disulphide bonds (C) Covalent bonds (D) Non-covalent bonds
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 : 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 : In denaturation of proteins, the bond which is not broken: (A) Disulphide bond (B) Peptide bond (C) Hydrogen bond (D) Ionic bond
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 : 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 : 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 : Hydrophobic bonds are formed in protein be- tween which amino acids?
Last Answer : Valine, leucine and isoleucine residues.
Description : Indole group of tryptophan responses positively to (A) Glyoxylic acid (B) Schiff’s reagent (C) Biuret test (D) Resorcinol test
Description : The useful reagent for detection of amino acids is (A) Molisch reagent (B) Dichlorophenol Indophenol (C) Ninhydrin (D) Biuret
Description : Biuret test is specific for (A) Two peptide linkage (B) Phenolic group (C) Imidazole ring (D) None 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 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 : 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 : 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 : What are the Reaction of amino acid using ninhydrin and biuret reagent?
Last Answer : What is the answer ?
Description : Which bond is present in the primary structure of protein? (A) Ester (B) Hydrogen (C) Ionic bond (D) Peptide
Description : Which method of protein estimation is depen- dent on the intact peptide bond?
Last Answer : Biuret method.
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 : The number of intra-chain disulphide bonds in pro-insulin: (A) One (B) Two (C) Three (D) Four
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 : 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 : 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 : The disulphide bond is not broken under the usual conditions of (A) Filtration (B) Reduction (C) Oxidation (D) Denaturation
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 : Assertion `:` Removal of gall bladder does affect the protein digestion. Reason `:` Bile juice break the peptide bond.
Last Answer : Assertion `:` Removal of gall bladder does affect the protein digestion. Reason `:` Bile juice break ... . D. If both Assertion & Reason are false.
Description : Assertion `:` Pancreatic amylase digest protein to amino acid. Reason `:` Pancreatic amylase breaks the peptide bond of protein.
Last Answer : Assertion `:` Pancreatic amylase digest protein to amino acid. Reason `:` Pancreatic amylase breaks the ... D. If both Assertion & Reason are false.
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 : 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 : Chloramphenicol inhibits bacterial protein synthesis by: A. Binding to 30S ribosome and inhibiting attachment of aminoacyl tRNA B. Binding to 50S ribosome and preventing peptide bond formation C. Binding to ... chain D. Binding to both 30S and 50S ribosome and inducing misreading of mRNA code
Last Answer : B. Binding to 50S ribosome and preventing peptide bond formation
Description : Insulin is a protein which controls (A) Blood clotting (B) Metabolic pathway (C) Digestion (D) Kreb’s cycle
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 : Ninhydrin reaction gives a purple colour and evolves CO2 with (A) Peptide bonds (B) Histamine (C) Ergothioneine (D) Aspargine
Description : The hydrogen bonds between peptide linkages are interfered by (A) Guanidine (B) Uric acid (C) Salicylic acid (D) Oxalic acid
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 : 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 : 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