Abstract
Solid-state NMR is a versatile and powerful tool for determining the dynamic structure of membrane proteins at atomic resolution. I review the recent progress in determining the orientation, the internal and global protein dynamics, the oligomeric structure, and the ligand-bound structure of membrane proteins with both alpha-helical and beta sheet conformations. Examples are given that illustrate the insights into protein function that can be gained from the NMR structural information.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, Non-P.H.S.
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Review
MeSH terms
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Animals
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Anisotropy
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Cell Membrane / metabolism
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Dose-Response Relationship, Drug
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Humans
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Ligands
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Magnetic Resonance Spectroscopy / methods*
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Membrane Proteins / chemistry
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Membrane Proteins / physiology*
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Models, Molecular
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Peptides / chemistry
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Potassium / chemistry
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Potassium Channels / chemistry
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Protein Conformation
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Protein Structure, Secondary
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Proteins / chemistry
Substances
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Ligands
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Membrane Proteins
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Peptides
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Potassium Channels
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Proteins
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Potassium