Journal
CHEMICAL COMMUNICATIONS
Volume 54, Issue 64, Pages 8917-8920Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c8cc03977a
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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.
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