Conformational switching in a light-harvesting protein as followed by single-molecule spectroscopy.

ABSTRACT: Among the ultimate goals of protein physics, the complete, experimental description of the energy paths leading to protein conformational changes remains a challenge. Single protein fluorescence spectroscopy constitutes an approach of choice for addressing protein dynamics, and, among naturally fluorescing proteins, light-harvesting (LH) proteins from purple bacteria constitute an ideal object for such a study. LHs bind bacteriochlorophyll a molecules, which confer on them a high intrinsic fluorescence yield. Moreover, the electronic properties of these pigment-proteins result from the strong excitonic coupling between their bound bacteriochlorophyll a molecules in combination with the large energetic disorder due to slow fluctuations in their structure. As a result, the position and proba

SUBMITTER: Gall A 

PROVIDER: S-EPMC4457476 | biostudies-literature | 2015 Jun

REPOSITORIES: biostudies-literature