Solution-Based Single-Molecule FRET Studies of K(+) Channel Gating in a Lipid Bilayer.

ABSTRACT: Ion channels are dynamic multimeric proteins that often undergo multiple unsynchronized structural movements as they switch between their open and closed states. Such structural changes are difficult to measure within the context of a native lipid bilayer and have often been monitored via macroscopic changes in Förster resonance energy transfer (FRET) between probes attached to different parts of the protein. However, the resolution of this approach is limited by ensemble averaging of structurally heterogeneous subpopulations. These problems can be overcome by measurement of FRET in single molecules, but this presents many challenges, in particular the ability to control labeling of subunits within a multimeric protein with acceptor and donor fluorophores, as well as the requirement to ima

SUBMITTER: Sadler EE 

PROVIDER: S-EPMC4919593 | biostudies-literature | 2016 Jun

REPOSITORIES: biostudies-literature