The effects of isolated N-methylated residues on the conformational characteristics of polypeptides

✍ Scribed by Alan E. Tonelli

• Publisher: Wiley (John Wiley & Sons)
• Year: 1976
• Tongue: English
• Weight: 325 KB
• Volume: 15
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.1976.360150814

✦ Synopsis

Abstract

Conformational energies have been estimated for the tripeptide fragments L‐Ala‐N‐methyl‐L‐Ala‐L‐Ala, L‐Ala‐L‐Ala‐N‐methyl‐L‐Ala, L‐Ala‐Sar‐L‐Ala, and L‐Ala‐Gly‐N‐methyl‐L‐Ala. The peptide bonds connecting L‐Ala and Gly with N‐methyl‐L‐Ala and L‐Ala with Sar were permitted to adopt the planar cis as well as the usual trans conformation. Contour maps of the conformational energies of the central residue in these tripeptide fragments are presented and compared to the conformational energy maps previously calculated for unmethylated L‐Ala and Gly surrounded by residues which are also unmethylated. In generl it is observed that L‐Ala and Gly residues that are either N‐methylated in their conformational freedom relative to the same residues in an unmethylated polypeptide chain.