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无规卷曲的概念。肽和变性蛋白质中的残余结构。

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

作者信息

Smith L J, Fiebig K M, Schwalbe H, Dobson C M

机构信息

Oxford Centre for Molecular Sciences and New Chemistry Laboratory, University of Oxford, UK.

出版信息

Fold Des. 1996;1(5):R95-106. doi: 10.1016/S1359-0278(96)00046-6.

DOI:10.1016/S1359-0278(96)00046-6
PMID:9080177
Abstract

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 non-native states emerging from rapid advances in experimental techniques involves comparison with a "random coll' 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. In particular, we focus on the description of a random coil in terms of statistical distributions in psi, phi 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.

摘要

由于蛋白质的非天然状态与蛋白质折叠、转运和稳定性等问题相关,因此越来越受到关注。实验技术的迅速发展产生了大量关于非天然状态的实验数据,解释这些数据的一个框架涉及与“随机卷曲”状态进行比较,随机卷曲状态除了局部相互作用所固有的结构外不具有其他结构。我们在此回顾随机卷曲的概念,从其整体性质到局部性质。特别地,我们关注根据ψ、φ空间中的统计分布对随机卷曲的描述。我们表明,这样一个模型与实验数据相结合,能够深入了解多肽链的结构性质,对于理解蛋白质折叠和分子设计具有重要意义。

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The concept of a random coil. Residual structure in peptides and denatured proteins.无规卷曲的概念。肽和变性蛋白质中的残余结构。
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Analysis of main chain torsion angles in proteins: prediction of NMR coupling constants for native and random coil conformations.蛋白质主链扭转角分析:天然和无规卷曲构象的核磁共振耦合常数预测
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Side-chains in native and random coil protein conformations. Analysis of NMR coupling constants and chi1 torsion angle preferences.天然和无规卷曲蛋白质构象中的侧链。核磁共振耦合常数及χ1扭转角偏好性分析。
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[Study of the compact denatured state of a protein by molecular dynamics simulation].
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