换一批
换一批Intrinsic flexibility of NLRP pyrin domains is a key factor in their conformational dynamics, fold stability, and dimerization.
第一作者：
Roland G,Huber
第一单位：
Institute for General, Inorganic and Theoretical Chemistry, Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck, Innrain, 80/82, Innsbruck, Austria; Bioinformatics Institute, Agency for Science, Technology and Research (A*STAR), 30 Biopolis Street #07-01 Matrix, Singapore, 138671.
作者：
主题词
衔接蛋白质类, 信号转导(Adaptor Proteins, Signal Transducing);人类(Humans);分子动力学模拟(Molecular Dynamics Simulation);突变(Mutation);核苷三磷酸酶(Nucleoside-Triphosphatase);蛋白质构象(Protein Conformation);蛋白质折叠(Protein Folding);蛋白质多聚化(Protein Multimerization);蛋白质结构, 三级(Protein Structure, Tertiary);阻遏蛋白质类(Repressor Proteins)
DOI
10.1002/pro.2601
PMID
25403012
发布时间
2020-12-09
- 浏览10
Protein science
174-81页
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