Hydrogen Bonds Determining the Conformation of Isolated Amino Acid Residues in Proteins: Re-Examination of the Fully Extended C5 Structures.

Authors

Marimuthu Vijayasarathy, Padmanabhan Balaram

Published in

Journal of peptide science : an official publication of the European Peptide Society. Volume 32. Issue 11. Pages e70131.

Abstract

Hydrogen bonds contribute substantially to the stabilisation of specific three-dimensional structures of peptides. The C5 hydrogen bond is an intraresidue interaction, which appears to contribute to the stabilisation of fully extended residue conformations, with backbone torsion angles (φ, ψ) lying close to ±180°. The present study revisits the occurrence of C5 conformations in proteins, using a high-resolution, non-homologous dataset of 6924 x-ray diffraction structures (sequence identity < 30%, resolution < 1.6 Å). Gly emerges as the residue with the highest propensity to adopt C5 conformations, followed by Ser. Residues with branched sidechains Leu, Val and Ile are strongly disfavoured. Specific examples in protein structures that have contiguous residues in C5 conformations are highlighted.

PMID:
42760859
Bibliographic data and abstract were imported from PubMed on 19 Sep 2026.

Read full publication at:
Please sign in to see all details.

Stats

1-terrible, 9-excellent. How would you rate this publication? Sign in in to submit your rating.

Post a comment

You need to be signed in to post comments. You can sign in here.

Comments

There are no comments yet.