α-helix is stabilized by (A) Hydrogen bonds (B) Disulphide bonds (C) Salt bonds (D) Non-polar bonds

1 Answer

Answer :

Answer : A

Related questions

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 : α-Helix is formed by (A) Hydrogen bonds (B) Hydrophobic bonds (C) Electrostatic bonds (D) Disulphide bonds

Last Answer : Answer : A

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 : 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 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 : 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 : In many proteins the hydrogen bonding produces a regular coiled arrangement which is called as (A) β-Helix (B) α-Helix (C) Both (A) and (B) (D) Spiral

Last Answer : Answer : B

Description : In many proteins the hydrogen bonding produces a regular coiled arrangement called (A) α-helix (B) β-helix (C) Both (A) and (B) (D) None of these

Last Answer : Answer : A

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 : 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 α-Helix is held in a coiled conformation partially because of : (a) Optical activity (b) Hydrogen bonding (c) Resonance (d) Delocalization

Last Answer : Hydrogen bonding

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

Last Answer : Answer : A

Description : The number of intra-chain disulphide bonds in pro-insulin: (A) One (B) Two (C) Three (D) Four

Last Answer : Answer : C

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 : In protein structure the α-helix and βpleated sheets are example of (A) Primary structure (B) Secondary structure (C) Tertiary structure (D) Quaternary structure

Last Answer : Answer : B

Description : α-helix is disrupted by certain amino acids like (A) Proline (B) Arginine (C) Histidine (D) Lysine

Last Answer : Answer : A

Description : The distance travelled per turn of α-helix in nm is (A) 0.34 (B) 0.44 (C) 0.54 (D) 0.64

Last Answer : Answer : C

Description : Each turn of α-helix contains the number of amino acids (A) 2.8 (B) 3.2 (C) 3.4 (D) 3.6

Last Answer : Answer : D

Description : An amino acid that does not take part in α helix formation is (A) Histidine (B) Tyrosine (C) Proline (D) Tryptophan

Last Answer : Answer : C

Description : Both α-helix and β-pleated sheet conformation of proteins were proposed by (A) Watson and Crick (B) Pauling and Corey (C) Waugh and King (D) Y.S.Rao

Last Answer : Answer : B

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

Last Answer : Answer : B

Description : Along the α-helix each amino acid residue advances in nm by (A) 0.15 (B) 0.10 (C) 0.12 (D) 0.20

Last Answer : Answer : A

Description : Each turn of α-helix contains the amino acid residues (number): (A) 3.6 (B) 3.0 (C) 4.2 (D) 4.5

Last Answer : Answer : A

Description : Which of the following is not a correct statement concerning the FriedelCrafts acylation of benzene? (a) An alkyl group substitutes for a hydrogen. (b) The benzene ring attacks an acylium ion. (c) The acylium ion is resonance stabilized. (d) The acylium ion is often produced from an acyl chloride.

Last Answer : An alkyl group substitutes for a hydrogen

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 : If oxygen which has an electronegativity of 3.5 bonds with hydrogen which has an electronegativity of 2.1 the bond between the two atoms will be classified as a polar what bond?

Last Answer : Need answer

Description : What is the difference between hydrogen bonds and polar bonds?

Last Answer : Covalent - equal sharing of generally one pair of electrons (e.g. H2 hydrogen molecule)Polar covalent- ubequal sharing - the more electronegative element "attracts " the electrons in the bond towards ... covakently bonded to one atom attracted to a very electrnegative atom. (Example is water, H2O)

Description : What is the difference between hydrogen bonds and polar bonds?

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Description : The α-Helix is a common form of (a) Primary structure (b) Tertiary structure (c) Secondary structure (d) None of these

Last Answer : Secondary structure

Description : The primary structure of a protein refers to : (a) whether the protein is fibrous or globular (b) the amino acid sequence in the polypeptide chain (c) the orientation of the amino acid side chains in space (d) the presence or absence of an α-helix

Last Answer : the amino acid sequence in the polypeptide chain

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