Correlating lipid bilayer fluidity with sensitivity and resolution of polytopic membrane protein spectra by solid-state NMR spectroscopy.

ABSTRACT: Solid-state NMR spectroscopy has emerged as an excellent tool to study the structure and dynamics of membrane proteins under native-like conditions in lipid bilayers. One of the key considerations in experimental design is the uniaxial rotational diffusion of the protein that can affect the NMR spectral observables. In this regard, temperature plays a fundamental role in modulating the phase properties of the lipids, which directly influences the rotational diffusion rate of the protein in the bilayer. In fact, it is well established that below the main phase transition temperature of the lipid bilayer the protein's motion is significantly slowed while above this critical temperature the rate is increased. In this article, we carried out a systematic comparison of the signal intensity and

SUBMITTER: Banigan JR 

PROVIDER: S-EPMC4438312 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature