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 : 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 : 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 : Pre-proinsulin contains a signal sequence having (A) 9 amino acid residues (B) 19 amino acid residues (C) 27 amino acid residues (D) 33 amino acid residues
Last Answer : Answer : B
Description : α-helix is disrupted by certain amino acids like (A) Proline (B) Arginine (C) Histidine (D) Lysine
Description : The distance travelled per turn of α-helix in nm is (A) 0.34 (B) 0.44 (C) 0.54 (D) 0.64
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
Description : Number of amino acid residues in glucagons is (A) 29 (B) 34 (C) 51 (D) 84
Description : The number of amino acid residues in PTH: (A) 51 (B) 84 (C) 90 (D) 115
Description : Number of amino acid residues in prolactin is (A) 51 (B) 84 (C) 191 (D) 198
Description : Number of amino acid residues in human growth hormone is (A) 51 (B) 84 (C) 191 (D) 198
Description : The number of amino acid residues in preproinsulin is (A) 51 (B) 84 (C) 109 (D) 119
Description : The number of amino acid residues in calcitonin in (A) 9 (B) 32 (C) 51 (D) 84
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 : Glycoproteins are marked for destruction by removal of their (A) Oligosaccharide prosthetic group (B) Sialic acid residues (C) Mannose residues (D) N-terminal amino acids
Description : Amino acid residues which are essential for the biological activity of PTH are (A) N-terminal 34 amino acids (B) N-terminal 50 amino acids (C) C-terminal 34 amino acids (D) C-terminal 50 amino acids
Description : Insulin is made up of (A) A single polypeptide chain having 51 amino acid residues (B) A single polypeptide chain having 84 amino acid residues (C) A-chain having 21 and B-chain having 30 amino acid residues (D) A-chain having 30 and B-chain having 21 amino acid residues
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 : 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 : 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
Description : α-helix is stabilized by (A) Hydrogen bonds (B) Disulphide bonds (C) Salt bonds (D) Non-polar bonds
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
Description : α-Helix is formed by (A) Hydrogen bonds (B) Hydrophobic bonds (C) Electrostatic bonds (D) Disulphide bonds
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
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 : 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 : how many amino acids are there in one turn of alpha helix?
Last Answer : 3.6 amino acid.
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 : The nucleophilic attack on the esterified carboxyl group of the peptidyl-tRNA occupying the P site and the α-amino group of the new amino acyl tRNA, the number of ATP required by the amino acid on the charged tRNA is (A) Zero (B) One (C) Two (D) Four
Description : In the biosynthesis of the iron protoporphyrin, the product of the condensation between succinyl-CoA and glycine is (A) α-Amino β-ketoadipic acid (B) δ-Aminolevulinate (C) Hydroxymethylbilane (D) Uroporphyrinogen I
Description : All of the following intermediates of citric acid cycle can be formed from amino acids except (A) α-Ketoglutarate (B) Fumarate (C) Malate (D) Oxaloacetate
Description : All α-amino acids have one asymmetric carbon atom except (A) Arginine (B) Glycine (C) Aspartic acid (D) Histidine
Description : The following ketoacid is involved in fixing dietary NH3 into amino acid: (A) Pyruvate (B) Oxalo acetate (C) Oxalo succinate (D) α-keto glutarate
Description : An example of α-amino acid not present in proteins but essential in mammalian metabolism is (A) 3-Amino 3-hydroxypropanoic acid (B) 2-Amino 3-hydroxybutanoic acid (C) 2-Amino 4-mercaptobutanoic acid (D) 2-Amino 3-mercaptopropanoic acid
Description : Are both sides of the DNA helix used for the same amino acid?
Last Answer : Typically only one strand is used as the template for messenger RNA synthesis, but some regions of DNA can encode multiple RNAs that are transcribed from opposite strands.
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 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 : Which of the following may characterize the “secondary structure” of proteins? (a) conformation of the protein backbone (b) α-Helix (c) parallel β-pleated sheet (d) all of the above
Last Answer : all of the above
Description : Proteins which interact with DNA and affect the rate of transcription possess the following structural motif: (A) Helix-turn-helix motif (B) Zinc finger motif (C) Leucine zipper motif (D) All of these
Description : Ten base pairs are present in one turn of the helix in (A) A-DNA (B) B-DNA (C) C-DNA (D) Z-DNA
Description : Thyroid stimulating hormone is a dimer. The α-subunits of TSH, LH, FSH are identical. Thus the biological specificity must therefore be β subunit in which the number of amino acids is (A) 78 (B) 112 (C) 130 (D) 199
Description : Glycosphingolipids are a combination of (A) Ceramide with one or more sugar residues (B) Glycerol with galactose (C) Sphingosine with galactose (D) Sphingosine with phosphoric acid
Description : All of the following are required for hydroxylation of proline residues except (A) Ascorbic acid (B) Glutamate (C) Ferrous ions (D) Molecular oxygen
Description : Which one of the following statements concerning glutamine is correct? (A) Contains three tetratable groups (B) Is classified as an acidic amino acid (C) Contains an amide group (D) Migrates to the cathode during electrophoresis at pH 7.0
Description : Zinc finger motif is formed in some proteins by binding of zinc to (A) Two cysteine residues (B) Two histidine residues (C) Two arginine residues (D) Two cysteine and two histidine residues or two pairs of two cysteine residues each
Description : In thyroxine, tyrosine residues are iodinated at positions: (A) 1 and 3 (B) 2 and 4 (C) 3 and 5 (D) 4 and 6
Description : Which of the following gives a positive Ninhydrin test? (A) Reducing sugar (B) Triglycerides (C) α-amino acids (D) Phospholipids
Description : For synthesis of CTP and UTP, the amino group comes from (A) Amide group of Asparagine (B) Amide group of glutamine (C) α-Amino group of glutamine (D) α-Amino group of glutamate
Description : The α-amino group of the new amino acyl tRNA in the A site carries out a nucleophilic attack on the esterified carboxyl group of the peptidyl tRNA occupying the P site. This reaction is catalysed by (A) DNA polymerase (B) RNA polymerase (C) Peptidyl transferase (D) DNA ligase