| Literature DB >> 25681966 |
Abstract
The native environment for a membrane protein is a phospholipid bilayer. Because the protein is immobilized on NMR timescales by the interactions within a bilayer membrane, solid-state NMR methods are essential to obtain high-resolution spectra. Approaches have been developed for both unoriented and oriented samples, however, they all rest on the foundation of the most fundamental aspects of solid-state NMR, and the chemical shift and homo- and hetero-nuclear dipole-dipole interactions. Solid-state NMR has advanced sufficiently to enable the structures of membrane proteins to be determined under near-native conditions in phospholipid bilayers.Entities:
Keywords: Bilayers; Chemical shift anisotropy; Dipolar coupling; Magic angle spinning; Phospholipids; Structure determination
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Year: 2014 PMID: 25681966 PMCID: PMC4372479 DOI: 10.1016/j.jmr.2014.11.015
Source DB: PubMed Journal: J Magn Reson ISSN: 1090-7807 Impact factor: 2.229