title: Dynamic nuclear polarization methods in solids and solutions to explore membrane proteins and membrane systems.
abstract: 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.
authors: Department of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106, USA.
authors: Chi-Yuan
authors: CY
authors: Cheng
authors: Songi
authors: S
authors: Han
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods; D031541:Fluorescence Resonance Energy Transfer / Q000379:methods; D006801:Humans; D008563:Membrane Lipids / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D014867:Water / Q000737:chemistry
chemical_list: D008563:Membrane Lipids; D008565:Membrane Proteins; D014867:Water