CheShift-2: graphic validation of protein structures
CheShift-2: graphic validation of protein structures
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DOI：
10.1093/bioinformatics/bts179
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发表时间：
2012-06-01
期刊：
影响因子：
5.8
通讯作者：
Scheraga, Harold A.
中科院分区：
文献类型：
--
作者：
Martin, Osvaldo A.;Vila, Jorge A.;Scheraga, Harold A.
观察到的和预测的C-13（α）化学位移之间的差异可以用作灵敏的探针，以检测蛋白质结构中可能的局部缺陷。出于这个原因，我们之前介绍了CheShift，一个用于蛋白质结构验证的Web服务器。现在，我们提出CheShift-2，其中实现了图形用户界面，使这种局部缺陷很容易看到。一系列的应用程序，以15个合奏的构象说明的能力CheShift-2快速，准确地定位的主要结构缺陷的每个残留物的基础上。由于准确性在CheShift预测中起着核心作用，因此通过探索CheShift-2中应使用哪种形式的组氨酸来研究组氨酸（His）的治疗。
The differences between observed and predicted C-13(alpha) chemical shifts can be used as a sensitive probe with which to detect possible local flaws in protein structures. For this reason, we previously introduced CheShift, a Web server for protein structure validation. Now, we present CheShift-2 in which a graphical user interface is implemented to render such local flaws easily visible. A series of applications to 15 ensembles of conformations illustrate the ability of CheShift-2 to locate the main structural flaws rapidly and accurately on a per-residue basis. Since accuracy plays a central role in CheShift predictions, the treatment of histidine ( His) is investigated here by exploring which form of His should be used in CheShift-2.