Solid-state NMR analysis of membrane proteins and protein aggregates by proton detected spectroscopy.

ABSTRACT: Solid-state NMR has emerged as an important tool for structural biology and chemistry, capable of solving atomic-resolution structures for proteins in membrane-bound and aggregated states. Proton detection methods have been recently realized under fast magic-angle spinning conditions, providing large sensitivity enhancements for efficient examination of uniformly labeled proteins. The first and often most challenging step of protein structure determination by NMR is the site-specific resonance assignment. Here we demonstrate resonance assignments based on high-sensitivity proton-detected three-dimensional experiments for samples of different physical states, including a fully-protonated small protein (GB1, 6 kDa), a deuterated microcrystalline protein (DsbA, 21 kDa), a membrane protein (Ds

SUBMITTER: Zhou DH 

PROVIDER: S-EPMC3484199 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature