Molecular orbital calculations on the conformation of polypeptides and proteins. 8. The conformational energy maps and stereochemical rotational states of the asparaginyl, glutaminyl aspartyl and glutamyl residues.

Abstract

AbstractQuantum‐mechanical calculations on the conformational energy map and stereo‐chemical rotational states of aminoacid residues by the PCILO method are extended to the asparaginyl, glutaminyl, aspartyl and glutamyl residues in their neutral form. One of the most outstanding features of the results is the occurrence of the global minimum (or of one of a few equivalent global minima) in the region of the left handed α‐helix for the first three of the above mentioned residues. The results of the calculations are compared with experimental data from eight, globular proteins which confirm that these residues may exist, in fact, in this conformation. They also enable to understand the experimentally observed possibility of helix reversal in esters of poly‐L‐aspartic acid as a function of substitutions in the side chain.