Ontology highlight
ABSTRACT:
SUBMITTER: Wang S
PROVIDER: S-EPMC3145272 | biostudies-literature | 2011 Aug
REPOSITORIES: biostudies-literature
Wang Shenlin S Shi Lichi L Kawamura Izuru I Brown Leonid S LS Ladizhansky Vladimir V
Biophysical journal 20110801 3
Solid-state NMR spectroscopy is an efficient tool for following conformational dynamics of membrane proteins at atomic resolution. We used this technique for the site-specific detection of light-induced hydrogen-deuterium exchange in the lipid-embedded heptahelical transmembrane photosensor Anabaena sensory rhodopsin to pinpoint the location of its conformational changes upon activation. We show that the light-induced conformational changes result in a dramatic, but localized, increase in the ex ...[more]