Optimized phospholipid bilayer nanodiscs facilitate high-resolution structure determination of membrane proteins.

ABSTRACT: Structural studies of membrane proteins are still hampered by difficulties of finding appropriate membrane-mimicking media that maintain protein structure and function. Phospholipid nanodiscs seem promising to overcome the intrinsic problems of detergent-containing environments. While nanodiscs can offer a near-native environment, the large particle size complicates their routine use in the structural analysis of membrane proteins by solution NMR. Here, we introduce nanodiscs assembled from shorter ApoA-I protein variants that are of markedly smaller diameter and show that the resulting discs provide critical improvements for the structure determination of membrane proteins by NMR. Using the bacterial outer-membrane protein OmpX as an example, we demonstrate that the combination of small n

SUBMITTER: Hagn F 

PROVIDER: S-EPMC3566289 | biostudies-literature | 2013 Feb

REPOSITORIES: biostudies-literature