Energy landscape of a Kv channel revealed by temperature steps while perturbing its electromechanical coupling.

ABSTRACT: Voltage-dependent potassium channels (Kv) play a crucial role in membrane repolarization during action potentials. They undergo voltage-dependent structural conformational transitions according to their distribution across their energy landscape. Understanding these transitions helps us comprehend their molecular function. Here, we used sudden and sustained temperature changes (Tstep) combined with different voltage protocols and mutations to dissect the energy landscape of the Shaker K⁺ channel. We used two mutations, ILT (V369I, I372L, and S376T) and I384N, that affect the coupling between the voltage sensor (VSD) and the pore domain (PD), to obtain the temperature dependence of VSD last transition and the intrinsic temperature dependence of the pore, respectively. Our finding

SUBMITTER: Pinto-Anwandter BI 

PROVIDER: S-EPMC11982254 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature