Microsecond protein dynamics observed at the single-molecule level.

ABSTRACT: How polypeptide chains acquire specific conformations to realize unique biological functions is a central problem of protein science. Single-molecule spectroscopy, combined with fluorescence resonance energy transfer, is utilized to study the conformational heterogeneity and the state-to-state transition dynamics of proteins on the submillisecond to second timescales. However, observation of the dynamics on the microsecond timescale is still very challenging. This timescale is important because the elementary processes of protein dynamics take place and direct comparison between experiment and simulation is possible. Here we report a new single-molecule technique to reveal the microsecond structural dynamics of proteins through correlation of the fluorescence lifetime. This method, two-dim

SUBMITTER: Otosu T 

PROVIDER: S-EPMC4506535 | biostudies-literature | 2015 Jul

REPOSITORIES: biostudies-literature