Answers are grounded in this paper and cite their sources.
Unusual p K a values for amino acids in the active sites of proteins play a large role in their function. A new explanation for these p K a shifts, which considers not electrostatic but mainly hydrophobic interactions as the cause, is presented here. This is substantiated by the correlation between the titrimetrically determined p K a values of a family of polypentapeptides containing aspartic acid and the aspartic acid content in the polypeptide.
No takes yet. Share an insight, caveat, or question.
Urry et al. (1993) studied this question.
Synapse has enriched 10 related papers. Consider them for comparative context: