Description : Primary structure of a protein is formed by (A) Hydrogen bonds (B) Peptide bonds (C) Disulphide bonds (D) All of these
Last Answer : Answer : B
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 : 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 : A protein reacts with biuret reagent which indicates 2 or more (A) Blood clotting (B) Peptide bond (C) Disulphide bonds (D) Hydrophobic bonds
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
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
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 : 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 : 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 : 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 : 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 : In denaturation of proteins, the bond which is not broken: (A) Disulphide bond (B) Peptide bond (C) Hydrogen bond (D) Ionic bond
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 : 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 : 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 : What bonds hold together the Quaternary structure of protein? -Biology
Last Answer : answer:
Description : The number of intra-chain disulphide bonds in pro-insulin: (A) One (B) Two (C) Three (D) Four
Description : α-Helix is formed by (A) Hydrogen bonds (B) Hydrophobic bonds (C) Electrostatic bonds (D) Disulphide 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 : 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 : Find the false statement: (A) The relationship construct known as the weak relationship type was defined by Dey, Storey & Barron (1999). (B) A weak relationship occurs when two ... Ternary, Quaternary and Quintary relationships are shown through a series of application scenario's and vignette's
Last Answer : (C) Conceptual model is not accurate representation of "Universe of interest".
Description : All the following statements about epidermal growth factor are true except (A) It is a protein (B) It possess quaternary structure (C) Its receptor is made up of a single polypeptide chain (D) Its receptor possesses tyrosine kinase domain
Description : In protein structure the α-helix and βpleated sheets are example of (A) Primary structure (B) Secondary structure (C) Tertiary structure (D) Quaternary structure
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 : In proteins the α-helix and β-pleated sheet are examples of (A) Primary structure (B) Secondary structure (C) Tertiary structure (D) Quaternary structure
Description : What is meant by quaternary structure of a pro- tein?
Last Answer : Certain polypeptides will aggregate to form one functional protein. This is referred to as the qua- ternary structure.
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 : 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 : 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 : 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 : 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 : 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 : 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 : 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 : 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 : For _______ bonding, one or more electrons are transferred between atoms. a. hydrogen b. ionic c. peptide d. covalent
Last Answer : b. ionic
Description : Conversion of pepsinogen to pepsin is (A) Intra molecular rearrangement (B) Breaking of hydrogen bonds (C) Covalent modification (D) Polymerisation
Description : Enzymes which catalyse binding of two substrates by covalent bonds are known as (A) Lyases (B) Hydrolases (C) Ligases (D) Oxidoreductases
Description : If the difference in electronegativity values between two atoms is more than 2.0 non-polar covalent bonds generally form?
Last Answer : At this value an ionic bond is formed.
Description : Most covalent compounds (a) Behave like electrolytes in the molten state (b) Have high melting and boiling points (c) Are hard substances because of strong covalent bonds (d) Are more soluble in non-polar solvents than in polar solvents
Last Answer : Ans:(d)
Description : NaCI has _______. (1) Non-polar bonds (2) Polar covalent bonds (3) Metallic bonds (4) Ionic bonds
Last Answer : (4) Ionic bonds Explanation: Sodium Chloride, NaCl. The classic case of ionic bonding, the sodium chloride molecule forms by the ionization of sodium and chlorine atoms and the attraction of the resulting ions.