Thermodynamics of binding by calmodulin correlates with target peptide α-helical propensity.

Abstract

In this work, we have examined contributions to the thermodynamics of calmodulin (CaM) binding from the intrinsic propensity for target peptides to adopt an α-helical conformation. CaM target sequences are thought to commonly reside in disordered regions within proteins. Using the ability of TFE to induce α-helical structure as a proxy, the six peptides… (More)
DOI: 10.1002/prot.24215

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