期刊
ANNUAL REVIEW OF PHYSICAL CHEMISTRY, VOL 64
卷 64, 期 -, 页码 507-532出版社
ANNUAL REVIEWS
DOI: 10.1146/annurev-physchem-040412-110028
关键词
GPCRs; structural determination; magic-angle spinning; electron paramagnetic resonance; lipid-protein interactions; hydration dynamics
资金
- Direct For Mathematical & Physical Scien [1112572] Funding Source: National Science Foundation
- Division Of Chemistry [1112572] Funding Source: National Science Foundation
- NIH HHS [DP2 OD008702] Funding Source: Medline
Membrane proteins regulate vital cellular processes, including signaling, ion transport, and vesicular trafficking. Obtaining experimental access to their structures, conformational fluctuations, orientations, locations, and hydration in membrane environments, as well as the lipid membrane properties, is critical to understanding their functions. Dynamic nuclear polarization (DNP) of frozen solids can dramatically boost the sensitivity of current solid-state nuclear magnetic resonance tools to enhance access to membrane protein structures in native membrane environments. Overhauser DNP in the solution state can map out the local and site-specific hydration dynamics landscape of membrane proteins and lipid membranes, critically complementing the structural and dynamics information obtained by electron paramagnetic resonance spectroscopy. Here, we provide an overview of how DNP methods in solids and solutions can significantly increase our understanding of membrane protein structures, dynamics, functions, and hydration in complex biological membrane environments.
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