Salt effects on the conformational stability of the visual G-protein-coupled receptor rhodopsin.

ABSTRACT: Membrane protein stability is a key parameter with important physiological and practical implications. Inorganic salts affect protein stability, but the mechanisms of their interactions with membrane proteins are not completely understood. We have undertaken the study of a prototypical G-protein-coupled receptor, the α-helical membrane protein rhodopsin from vertebrate retina, and explored the effects of inorganic salts on the thermal decay properties of both its inactive and photoactivated states. Under high salt concentrations, rhodopsin significantly increased its activation enthalpy change for thermal bleaching, whereas acid denaturation affected the formation of a denatured loose-bundle state for both the active and inactive conformations. This behavior seems to correlate with changes

SUBMITTER: Reyes-Alcaraz A 

PROVIDER: S-EPMC3297775 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature