a) For most enzymes, the Km is closely related to the affinity of the enzyme for its substrate(s). Which has higher affinity, an enzyme with a low Km, or an enzyme with a high Km? Justify your answer.
b) True or false: at a pH equal to its pKA, the average charge on an ionizable amino acid sidechain (such as lysine's ε-amino group) will be zero.
c) Titration of isoleucine by a strong base, for example NaOH, reveals two pK’s. The titration reaction occurring at pK1 (pK1 = 2.4) is:
A) —COOH + OH−→ —COO−+ H2O.
B) —COOH + —NH2→ —COO−+ —NH2.
C) —COO−+ —NH2→ —COOH + —NH2.
D) —NH3++ OH−→ —NH2+ H2O.
E) —NH2+ OH−→ —NH− + H2O.
Circle the correct answer.
a) For most enzymes, the Km is closely related to the affinity of the enzyme for...
A is the correct answer but I'm not sure how to actually get to that answer. 20. The titration of fully protonated alanine (starting at pH - 1) by a strong base, for example NaOH, reveals two pa's. The titration reaction occurring at pK(pKi - 2.35) is: A) -COOH + OH -COO + H2O B) -COOH + -NH2 -COO + -NH, C) COO -NH - COOH + -NH2 D) -NH3 + OH -NH2 + H2O E) -NH2 + OH →...