Measuring membrane protein bond orientations in nanodiscs via residual dipolar couplings.

ABSTRACT: Membrane proteins are involved in numerous vital biological processes. To understand membrane protein functionality, accurate structural information is required. Usually, structure determination and dynamics of membrane proteins are studied in micelles using either solution state NMR or X-ray crystallography. Even though invaluable information has been obtained by this approach, micelles are known to be far from ideal mimics of biological membranes often causing the loss or decrease of membrane protein activity. Recently, nanodiscs, which are composed of a lipid bilayer surrounded by apolipoproteins, have been introduced as a more physiological alternative than micelles for NMR investigations on membrane proteins. Here, we show that membrane protein bond orientations in nanodiscs can be ob

SUBMITTER: Bibow S 

PROVIDER: S-EPMC4088969 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature