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

1 Answer

Answer :

Answer : C

Related questions

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 : 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 : Denaturation of proteins involves breakdown of (A) Secondary structure(B) Tertiary structure (C) Quarternary structure(D) All of these

Last Answer : Answer : D

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 : During denaturation of proteins, all of the following are disrupted except (A) Primary structure (B) Secondary structure (C) Tertiary structure (D) Quaternary structure

Last Answer : Answer : B

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 : 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

Last Answer : Answer : A

Description : Irreversible precipitation of proteins caused by heating is called : (a) Polymerisation (b) Denaturation (c) Electrophoresis (d) Inversion

Last Answer : Denaturation

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 : Which bond is present in the primary structure of protein? (A) Ester (B) Hydrogen (C) Ionic bond (D) Peptide

Last Answer : Answer : D

Description : In case of severe denaturation of protein, there is (A) Reversible denaturation (B) Moderate reversible denaturation (C) Irreversible denaturation (D) None of these

Last Answer : Answer : C

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 : 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

Last Answer : Answer : D

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Last Answer : Answer: a, b, c, d During the ischemia and hypoperfusion phase, degradation of ATP stores essential to maintain cell integrity and significant loss of diffusible ... either the neutrophil adhesive complex or the endothelial selectins dramatically lessens ischemia/reperfusion microvascular injury

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

Last Answer : Answer : B

Description : Digestion of proteins involves (a) changes in secondary structure only (b) cleavage of peptide linkages (c) removal of all carboxyl groups in the form of CO2. (d) removal of all NH2 groups in the form of NH3

Last Answer : cleavage of peptide linkages

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

Last Answer : Answer : B

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

Last Answer : Answer : C

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

Last Answer : Answer : D

Description : The hydrogen bonds between peptide linkages are interfered by (A) Guanidine (B) Uric acid (C) Salicylic acid (D) Oxalic acid

Last Answer : Answer : A

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 hydrogen bonds between peptide linkages of a protein molecules are interfered by (A) Guanidine (B) Uric acid (C) Oxalic acid (D) Salicylic acid

Last Answer : Answer : A

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 : In quaternary structure, subunits are linked by (A) Peptide bonds (B) Disulphide bonds (C) Covalent bonds (D) Non-covalent bonds

Last Answer : Answer : D

Description : Peptide bonds are found in: a) carbohydrates b) lipids c) nucleic acids d) proteins

Last Answer : ANSWER: D -- PROTEINS

Description : In a protein molecule the disulphide bond is not broken by (A) Reduction (B) Oxidation (C) Denaturation (D) X-ray diffraction

Last Answer : Answer : C

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

Last Answer : Answer : B

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 : 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 : Many globular proteins are stable in solution although they lack in (A) Hydrogen bonds (B) Salt bonds (C) Non-polar bonds (D) Disulphide bonds

Last Answer : Answer : D

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

Last Answer : Answer : A

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

Last Answer : Answer : D

Description : A protein reacts with biuret reagent which indicates 2 or more (A) Blood clotting (B) Peptide bond (C) Disulphide bonds (D) Hydrophobic bonds

Last Answer : Answer : B

Description : Ninhydrin reaction gives a purple colour and evolves CO2 with (A) Peptide bonds (B) Histamine (C) Ergothioneine (D) Aspargine

Last Answer : Answer : D

Description : Bonds that are formed between two cysteine residues is (A) Disulphide (B) Peptide (C) Electrostatic (D) Hydrophobic

Last Answer : Answer : A

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

Last Answer : Answer : C

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

Last Answer : Answer : C

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

Last Answer : Answer : A

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

Last Answer : Answer : A

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 : What is meant by denaturation in proteins? -Biology

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Description : From two amino acids peptide bond formation involves removal of one molecule of (A) Water (B) Ammonia (C) Carbondioxide (D) Carboxylic acid

Last Answer : Answer : A

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Description : If you were to open the entire molecule along the hydrogen bonds what bases would the left side attach to?

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Description : What is the maximum number of hydrogen bonds in a H2O molecule?

Last Answer : 4

Description : The angle between any two carbon-hydrogen bonds in a methane molecule is how many degrees?

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