4.3 Article

CheSPI: chemical shift secondary structure population inference

期刊

JOURNAL OF BIOMOLECULAR NMR
卷 75, 期 6-7, 页码 273-291

出版社

SPRINGER
DOI: 10.1007/s10858-021-00374-w

关键词

NMR; Protein; Order; Disorder; Chemical shifts

向作者/读者索取更多资源

CheSPI is a simple and efficient method that can accurately predict local structure and disorder, even in very small amounts of residual structure. It provides predictions for up to eight structural classes for structured regions and proteins, and generates intuitive numeric and graphical output.
NMR chemical shifts (CSs) are delicate reporters of local protein structure, and recent advances in random coil CS (RCCS) prediction and interpretation now offer the compelling prospect of inferring small populations of structure from small deviations from RCCSs. Here, we present CheSPI, a simple and efficient method that provides unbiased and sensitive aggregate measures of local structure and disorder. It is demonstrated that CheSPI can predict even very small amounts of residual structure and robustly delineate subtle differences into four structural classes for intrinsically disordered proteins. For structured regions and proteins, CheSPI provides predictions for up to eight structural classes, which coincide with the well-known DSSP classification. The program is freely available, and can either be invoked from URL as a web implementation, or run locally from command line as a python program. CheSPI generates comprehensive numeric and graphical output for intuitive annotation and visualization of protein structures. A number of examples are provided.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.3
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据