Dynamics of internal pore opening in K(V) channels probed by a fluorescent unnatural amino acid.

ABSTRACT: Atomic-scale models on the gating mechanism of voltage-gated potassium channels (Kv) are based on linear interpolations between static structures of their initial and final state derived from crystallography and molecular dynamics simulations, and, thus, lack dynamic structural information. The lack of information on dynamics and intermediate states makes it difficult to associate the structural with the dynamic functional data obtained with electrophysiology. Although voltage-clamp fluorometry fills this gap, it is limited to sites extracellularly accessible, when the key region for gating is located at the cytosolic side of the channels. Here, we solved this problem by performing voltage-clamp fluorometry with a fluorescent unnatural amino acid. By using an orthogonal tRNA-synthetase pai

SUBMITTER: Kalstrup T 

PROVIDER: S-EPMC3657800 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature