Energetics of angstrom-scale conformational changes in an RCK domain of the MthK K⁺ channel.

ABSTRACT: Allosteric proteins transition among different conformational states in a ligand-dependent manner. Upon resolution of a protein's individual states, one can determine the probabilities of these states, thereby dissecting the energetic mechanisms underlying their conformational changes. Here we examine individual regulator of conductance to K⁺ (RCK) domains that form the regulatory module of the Ca²⁺-activated MthK channel. Each domain adopts multiple conformational states differing on an ångström scale. The probabilities of these different states of the domain, assessed in different Ca²⁺ concentrations, allowed us to fully determine a six-state model that is minimally required to account for the energetic characteristics of the Ca²⁺-dependent con

SUBMITTER: Lewis JH 

PROVIDER: S-EPMC6822698 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature