Geometrical criteria for left-handed twists within protein beta-strands

Abstract : Using a statistical analysis on beta-sheet structures from the Protein Data Bank, characteristic angles within beta-strands were correlated to the nature of the side chains. The twists were computed from the atomic coordinates of five consecutive amino acids' alpha carbons from single beta-strand sequences. Conditions on the angles for twists to be mainly left-handed are given together with the frequency of occurrence for these non-standard geometrical properties within protein beta-strands. Applications in protein structure prediction and CASP challenges in particular are envisioned by making use of the probabilities of occurrence in protein structures of angle value ranges for given amino acids.
Type de document :
Article dans une revue
Journal of Biophysical Chemistry, 2014, 05 (01), pp.5 - 12. 〈10.4236/jbpc.2014.51002〉
Liste complète des métadonnées

https://hal-pasteur.archives-ouvertes.fr/pasteur-01414270
Contributeur : Maya Um <>
Soumis le : lundi 12 décembre 2016 - 11:22:42
Dernière modification le : jeudi 11 janvier 2018 - 06:26:03
Document(s) archivé(s) le : mardi 28 mars 2017 - 00:50:41

Fichier

150 - Jestin .pdf
Publication financée par une institution

Licence


Distributed under a Creative Commons Paternité 4.0 International License

Identifiants

Collections

Citation

Bernard Caudron, Jean-Luc Jestin. Geometrical criteria for left-handed twists within protein beta-strands. Journal of Biophysical Chemistry, 2014, 05 (01), pp.5 - 12. 〈10.4236/jbpc.2014.51002〉. 〈pasteur-01414270〉

Partager

Métriques

Consultations de la notice

142

Téléchargements de fichiers

126