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

作　　者：Bernard Caudron Jean-Luc Jestin 

机构地区：[1]Centre d'Informatique pour la Biologie, Institut Pasteur, Paris, France [2]Unité de Bioinformatique Structurale, Département de Biologie Structurale et Chimie, Institut Pasteur, Paris, France

出　　处：《Journal of Biophysical Chemistry》2014年第1期5-12,共8页生物物理化学（英文）

摘　　要：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.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.

关 键 词：BETA-SHEET PROTEIN Data Bank PROTEIN Backbone PROTEIN Structure Model Quality Assessment CASP 

分 类 号：R73[医药卫生—肿瘤]