期刊
CHEMICAL COMMUNICATIONS
卷 54, 期 64, 页码 8917-8920出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c8cc03977a
关键词
-
Herein we present the effect of artificially imposed topological constraint on calmodulin (CaM) backbone dynamics and its molecular recognition behavior. While backbone dynamics of CaM remain largely unperturbed, the thermodynamic profile of CaM binding to the smooth-muscle myosin light-chain kinase (smMLCK) peptide is modulated significantly.
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