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
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Protein science
174-81页
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