Racemization of Amino Acids in Dipeptides Shows COOH > NH2 for Non-Sterically Hindered Residues.
Science
; 207(4432): 765-7, 1980 Feb 15.
Article
en En
| MEDLINE
| ID: mdl-17796009
ABSTRACT
The relative rates of racemization for amino acid residues at the NH(2) and COOH ends of 37 different dipeptides were determined. In nine dipeptides containing alanine, leucine, phenylalanine, aspartic acid, and methionine, the amino acid residue racemized faster at the COOH-terminal position than at the NH(2)-terminal position (COOH > NH(2)). The sterically hindered amino acids isoleucine and valine showed NH(2) > COOH. Six proline dipeptides showed NH(2) > COOH. Intramolecular effects have been invoked to explain these surprising results.