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lüll Oligomeric structure, dynamics, and orientation of membrane proteins from solid-state NMR Hong MStructure 2006[Dec]; 14 (12): 1731-40Solid-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.|Animals[MESH]|Anisotropy[MESH]|Cell Membrane/metabolism[MESH]|Dose-Response Relationship, Drug[MESH]|Humans[MESH]|Ligands[MESH]|Magnetic Resonance Spectroscopy/*methods[MESH]|Membrane Proteins/chemistry/*physiology[MESH]|Models, Molecular[MESH]|Peptides/chemistry[MESH]|Potassium Channels/chemistry[MESH]|Potassium/chemistry[MESH]|Protein Conformation[MESH]|Protein Structure, Secondary[MESH]|Proteins/chemistry[MESH] |