Using chemical shifts to assess transient secondary structure and generate ensemble structures of intrinsically disordered proteins.
Using chemical shifts to assess transient secondary structure and generate ensemble structures of intrinsically disordered proteins.
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使用化学位移来评估瞬时二级结构并生成本质上无序的蛋白质的整体结构。
DOI：
10.1007/978-1-61779-927-3_11
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发表时间：
2012
期刊：
影响因子：
--
通讯作者：
Ytreberg,FMarty
中科院分区：
文献类型：
--
作者：
Kashtanov,Stepan;Borcherds,Wade;Wu,Hongwei;Daughdrill,GaryW;Ytreberg,FMarty
多肽中骨架原子的化学位移对二面角φ和psi敏感，并且可以用于估计瞬时二级结构和产生内在无序蛋白质（IDP）的结构系综。在本章中，几个随机线圈参考数据库用于估计瞬态二级结构进行了描述，并概述了使用这些数据库来估计瞬态二级结构的程序。还提出了一种新的协议，用于生成一个IDP的结构和重新加权这些结构，以优化模拟和实验化学位移值之间的配合不同的合奏。
The chemical shifts of backbone atoms in polypeptides are sensitive to the dihedral angles phi and psi and can be used to estimate transient secondary structure and to generate structural ensembles of intrinsically disordered proteins (IDPs). In this chapter, several of the random coil reference databases used to estimate transient secondary structure are described, and the procedure is outlined for using these databases to estimate transient secondary structure. A new protocol is also presented for generating a diverse ensemble of structures for an IDP and reweighting these structures to optimize the fit between simulated and experimental chemical shift values.