期刊
BIOINFORMATICS
卷 35, 期 3, 页码 462-469出版社
OXFORD UNIV PRESS
DOI: 10.1093/bioinformatics/bty635
关键词
-
类别
资金
- European Molecular Biology Laboratory
- Biotechnology and Biological Sciences Research Council [BB/N011600/1]
- Spanish Ministry of Economy and Competitiveness (MINECO) [BIO2016-79930-R]
- Interreg POCTEFA [EFA086/15]
- European Commission [676566]
- BBSRC [BB/N011600/1] Funding Source: UKRI
Motivation: Understanding the relationship between the sequence, structure, binding energy, binding kinetics and binding thermodynamics of protein-protein interactions is crucial to understanding cellular signaling, the assembly and regulation of molecular complexes, the mechanisms through which mutations lead to disease, and protein engineering. Results: We present SKEMPI 2.0, a major update to our database of binding free energy changes upon mutation for structurally resolved protein-protein interactions. This version now contains manually curated binding data for 7085 mutations, an increase of 133%, including changes in kinetics for 1844 mutations, enthalpy and entropy changes for 443 mutations, and 440 mutations, which abolish detectable binding.
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。
推荐
暂无数据