Which amino acid is ideal for the transfer of protons within the catalytic site of enzymes due to the presence of significant amounts of both the protonated and deprotonated forms of its side chain at biological pH?Answers: A. AlanineB. AsparagineC. TyrosineD. CysteineE. Histidine

Which of the following enzymes catalyzes the transpeptidation reaction linking amino acids in the growing polypeptide chain? A. Transpeptidase B. Peptidyl transferase C. Aminoacyl-tRNA synthetase D. Translocase

Which of the following amino acids has a negatively charged side chain at physiological pH?Group of answer choicesglutamineasparaginelysinemethionineglutamic acidarginine

Question 4Use the following key to answer the next questions:A. Using one letter code, write out the reaction scheme for the stepwise de-protonationof this amino acid from the fully protonated to the fully de-protonated form. Clearlyindicate the net charge of each form.B. Which of the above forms do not exist at any pH?C. Which form(s) would predominate after you added one mole of NaOH to one mole ofform ‘E’?D. Estimate the pH after you mixed equal molar amounts of A and D.

Draw an α amino acid with an ethyl −−CH2CH3 side chain. Draw the molecule as it would appear at physiological pH.

Which of the following amino acid undergoes oxidative deamination?