Peptide Conformations. I. Nuclear Magnetic Resonance Study of the Carbamate Reaction of Amino Acids and Peptides

Abstract

Nuclear magnetic resonance spectroscopy has been applied to the study of carbamate formation in solutions of amino acids and peptides in a carbonate-bicarbonate system. The possible conformations of these carbamates are discussed in terms of the n.m.r. data obtained. The n.m.r. parameters are reported for the diastereomers L-alanyl-L or D-phenylalanine and L-phenylalanyl-L or D-alanine and for the dipeptide glycyl-L-phenylalanine and their carbamates. The results are interpreted in terms of preferred rotamers about the Cα—Cβ bond of the phenylalanine residue and a β-type conformation of the peptide chain, wherein the two α-protons lie in the plane of the amide bond. All observations are in agreement with a shorter end to end distance in L,D- compared with L,L-dipeptides.