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仅使用氨基酸序列预测残基是否受氢交换保护的状态

Prediction of Residue Status to Be Protected or Not Protected From Hy-drogen Exchange Using Amino Acid Sequence Only.

作者信息

Nikita V Dovidchenko, Oxana V Galzitskaya

机构信息

Institute of Protein Research, Russian Academy of Sciences, Institutskaya str., 4 Pushchino, Moscow Region, 142290, Russia.

出版信息

Open Biochem J. 2008;2:77-80. doi: 10.2174/1874091X00802010077. Epub 2008 Jun 3.

Abstract

We have outlined here some structural aspects of local flexibility. Important functional properties are related to flexible segments. We try to predict regions that have been shown to exhibit the highest probability of being folded in the equilibrium intermediate or native state and will be protected from hydrogen exchange using amino acid sequence only. Our approach FoldUnfold for the prediction of unstructured regions has been applied to seven different proteins. For 80% of the residues considered in this paper we can predict correctly their status: will they be protected or not from hydrogen exchange. An additional goal of our study is to assess whether properties inferred using the bioinformatics approach are easily applicable to predict behavior of proteins in solution.

摘要

我们在此概述了局部灵活性的一些结构方面。重要的功能特性与柔性片段相关。我们试图仅利用氨基酸序列来预测那些在平衡中间体或天然状态下折叠概率最高且将免受氢交换影响的区域。我们用于预测非结构化区域的方法FoldUnfold已应用于七种不同的蛋白质。对于本文所考虑的80%的残基,我们能够正确预测它们的状态:它们是否会免受氢交换影响。我们研究的另一个目标是评估使用生物信息学方法推断出的特性是否易于应用于预测蛋白质在溶液中的行为。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb24/2570557/4d6a57b14e67/TOBIOCJ-2-77_F1.jpg

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