Conformational heterogeneity in closed and open states of the KcsA potassium channel in lipid bicelles.

ABSTRACT: The process of ion channel gating-opening and closing-involves local and global structural changes in the channel in response to external stimuli. Conformational changes depend on the energetic landscape that underlies the transition between closed and open states, which plays a key role in ion channel gating. For the prokaryotic, pH-gated potassium channel KcsA, closed and open states have been extensively studied using structural and functional methods, but the dynamics within each of these functional states as well as the transition between them is not as well understood. In this study, we used solution nuclear magnetic resonance (NMR) spectroscopy to investigate the conformational transitions within specific functional states of KcsA. We incorporated KcsA channels into lipid bicelles a

SUBMITTER: Kim DM 

PROVIDER: S-EPMC4969796 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature