Description : After formation of a peptide bond, mRNA is translocated along the ribosome by (A) eEF-1 and GTP (B) eEF-2 and GTP (C) Peptidyl transferase and GTP (D) Peptidyl transferase and ATP
Last Answer : Answer : B
Description : Select the antibiotic which inhibits bacterial protein synthesis by interfering with translocation of elongating peptide chain from acceptor site back to the peptidyl site of the ribosome so that ... chain is prematurely terminated: A. Chloramphenicol B. Erythromycin C. Tetracycline D. Streptomycin
Last Answer : B. Erythromycin
Description : Which one of the following also acts as a catalyst in a bacterial cell? (a) 5S rRNA (b) snRNA (c) hnRNA (d) 23S rRNA
Last Answer : (a) 5S rRNA
Description : Which of the following rRNAs acts as structural RNA as well as ribozyme in bacteria? (a) 5S rRNA (b) 18S rRNA (c) 23S rRNA (d) 5.8S rRNA
Last Answer : 23S rRNA
Last Answer : (c) 23S rRNA
Description : Erythromycin binds to 50 S ribosomal sub unit and (A) Inhibits binding of amino acyl tRNA (B) Inhibits Peptidyl transferase activity (C) Inhibits translocation (D) Causes premature chain termination
Last Answer : Answer : C
Description : Peptidyl transferase activity of 50 S ribosomal subunits is inhibited by (A) Rifampicin (B) Cycloheximide (C) Chloramphenicol (D) Erythromycin
Description : Peptidyl transferase activity is present in (A) 40 S ribosomal subunit (B) 60 S ribosomal subunit (C) eEF-2 (D) Amino acyl tRNA
Description : Peptidyl transferase activity is located in (A) Elongation factor (B) A charged tRNA molecule (C) Ribosomal protein (D) A soluble cytosolic protein
Description : Erythromycin acts on ribosomes and inhibit (A) Formation of initiation complex (B) Binding of aminoacyl tRNA (C) Peptidyl transferase activity (D) Translocation
Last Answer : Answer : D
Description : Streptomycin prevents synthesis of polypeptide by (A) Inhibiting initiation process (B) Releasing premature polypeptide (C) Inhibiting peptidyl transferase activity (D) Inhibiting translocation
Last Answer : Answer : A
Description : In prokaryotes, chloramphenicol (A) Causes premature release of the polypeptide chain (B) Causes misreading of the mRNA (C) Depolymerises DNA (D) Inhibits peptidyl transferase activity
Description : Translocation of the newly formed peptidyl tRNA at the A site into the empty P site involves (A) EF-II, GTP (B) EF-I, GTP (C) EF-I, GDP (D) Peptidyl transferase, GTP
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
Description : Which of the following step of translation does not consume a high energy phosphate bond? (a) Peptidyl transferase reaction (b) Aminoacyl tRNA binding to A-site (c) Translocation (d) Amino acid activation
Last Answer : (b) Aminoacyl tRNA binding to A-site
Last Answer : (a) Peptidyl transferase reaction
Description : Which of the following molecule catalyzes the transpeptidation reaction? A.RNA polymerase B.Peptidyl transferase C.DNA ligase D.DNA polymerase
Last Answer : B.Peptidyl transferase
Description : The enzyme amino acyl tRNA synthetase is involved in (A) Dissociation of discharged tRNA from 80S ribosome (B) Charging of tRNA with specific amino acids (C) Termination of protein synthesis (D) Nucleophilic attack on esterified carboxyl group of peptidyl tRNA
Description : Which binding is inhibited by pactamycin? A- Aminoacyl-tRNA to the A-site of 30S subunit B- Initiator-tRNA to 30S/40S initiation complexes C- Peptidyl t-RNA to the 50S subunit D- Formation of peptide bond in P site
Last Answer : Initiator-tRNA to 30S/40S initiation complexes
Description : In mammalian cells rRNA is produced mainly in the (A) Endoplasmic reticulum (B) Ribosome (C) Nucleolus (D) Nucleus
Last Answer : C
Description : The RNA that pick up specific amino acid from amino acid pool in the cytoplasm to ribosome during protein synthesis is called (a) rRNA (b) RNA (c) mRNA (d) tRNA.
Last Answer : a) rRNA
Description : The RNA that pick up specific amino acid from amino acid pool in the cytoplasm to ribosome during protein synthesis is called (a) rRNA (b) RNA (c) mRNA (d) tRNA
Last Answer : tRNA
Description : Biochemically the ribosome consists of _______________ and some 50 structural . (A) mRNA, Carbohydrates (B) tRNA, lipids (C) mRNA, Proteins (D) rRNA, Proteins
Last Answer : (D) rRNA, Proteins
Description : The most important mechanism by which gram negative bacilli acquire chloramphenicol resistance is (a) Decreased permeability into the bacterial cell (b) Acquisition of a plasmid encoded ... bacterial ribosome for chloramphenicol (d) Switching over from ribosomal to mitochondrial protein synthesis
Last Answer : Ans: B
Description : The most important mechanism by which gram negative bacilli acquire chloramphenicol resistance is: A. Decreased permeability into the bacterial cell B. Acquisition of a plasmid encoded ... the bacterial ribosome for chloramphenicol D. Switching over from ribosomal to mitochondrial protein synthesi
Last Answer : B. Acquisition of a plasmid encoded for chloramphenicol acetyl transferas
Description : A growing peptide in a ribosome can not be shifted to the adjacent ribosome because (A) It is firmly attached (B) It will get the amino acid cleaved (C) The gap between the ribosomes is too big for a shift (D) The adjacent ribosomes have different composition
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 : The mechanism of antibacterial action of tetracycline involves (a) Binding to a component of the 50S ribosomal subunit (b) Inhibition of translocase activity (c) Blockade of binding of ... (d) Selective inhibition of ribosomal peptidyl transferases (e) Inhibition of DNA-dependent RNA polymerase
Last Answer : Ans: C
Description : What happens at the ribosome in the production of a protein? a. mRNA brings the codon b. tRNA brings the anticodon c. the amino acids are linked by polypeptide bonds d. translation e. all the above
Last Answer : c. the amino acids are linked by polypeptide bonds
Description : How peptide bonds are formed? -Biology
Last Answer : answer:
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 : What organelles form peptide bonds between amino acids?
Last Answer : Ribosomes. They are constructed from protein themselves, but, more germane to the question, they are also partially composed of catalytic RNA, which forges the peptide bonds.
Description : What Peptide bonds form between the?
Last Answer : What is the answer ?
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 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 : A protein reacts with biuret reagent which indicates 2 or more (A) Blood clotting (B) Peptide bond (C) Disulphide bonds (D) Hydrophobic bonds
Description : Ninhydrin reaction gives a purple colour and evolves CO2 with (A) Peptide bonds (B) Histamine (C) Ergothioneine (D) Aspargine
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
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 : 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
Description : Bonds that are formed between two cysteine residues is (A) Disulphide (B) Peptide (C) Electrostatic (D) Hydrophobic
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 : Primary structure of a protein is formed by (A) Hydrogen bonds (B) Peptide bonds (C) Disulphide bonds (D) All of these
Description : In quaternary structure, subunits are linked by (A) Peptide bonds (B) Disulphide bonds (C) Covalent bonds (D) Non-covalent bonds