Transmembrane helix orientation and dynamics: insights from ensemble dynamics with solid-state NMR observables.

ABSTRACT: As the major component of membrane proteins, transmembrane helices embedded in anisotropic bilayer environments adopt preferential orientations that are characteristic or related to their functional states. Recent developments in solid-state nuclear magnetic resonance (SSNMR) spectroscopy have made it possible to measure NMR observables that can be used to determine such orientations in a native bilayer environment. A quasistatic single conformer model is frequently used to interpret the SSNMR observables, but important motional information can be missing or misinterpreted in the model. In this work, we have investigated the orientation of the single-pass transmembrane domain of viral protein "u" (VpuTM) from HIV-1 by determining an ensemble of structures using multiple conformer models ba

SUBMITTER: Jo S 

PROVIDER: S-EPMC3123920 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature