The concept of a random coil - Residual structure in peptides and denatured proteins

被引:200
作者
Smith, LJ
Fiebig, KM
Schwalbe, H
Dobson, CM
机构
[1] UNIV OXFORD,OXFORD CTR MOL SCI,OXFORD OX1 3QT,ENGLAND
[2] UNIV OXFORD,NEW CHEM LAB,OXFORD OX1 3QT,ENGLAND
来源
FOLDING & DESIGN | 1996年 / 1卷 / 05期
基金
英国惠康基金;
关键词
CONFORMATIONAL-DEPENDENT PROPERTIES; PANCREATIC TRYPSIN-INHIBITOR; X-RAY-SCATTERING; SECONDARY STRUCTURE; AMINO-ACIDS; STRUCTURE PREDICTION; HETERONUCLEAR NMR; COMPLETE SEQUENCE; MEAN-SQUARE; STATES;
D O I
10.1016/S1359-0278(96)00046-6
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Non-native states of proteins are of increasing interest because of their relevance to issues such as protein folding, translocation and stability. A framework for interpreting the wealth of experimental data for nonnative states emerging from rapid advances in experimental techniques involves comparison with a 'random coil' state, which possesses no structure except that inherent in the local interactions. We review here the concept of a random coil, from its global to its local properties. tn particular, we focus on the description of a random coil in terms of statistical distributions in phi,psi space. We show that such a model, in combination with experimental data, provides insight into the structural properties of polypeptide chains and has significance for understanding protein folding and for molecular design. (C) Current Biology Ltd
引用
收藏
页码:R95 / R106
页数:12
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