Oligomeric structure, dynamics, and orientation of membrane proteins from solid-state NMR.
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.
Hong
Mei
M
Department of Chemistry, Iowa State University, Ames, Iowa 50011, USA. mhong@iastate.edu <mhong@iastate.edu>
D000818:Animals; D016880:Anisotropy; D002462:Cell Membrane / Q000378:metabolism; D004305:Dose-Response Relationship, Drug; D006801:Humans; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008565:Membrane Proteins / Q000737:chemistry / Q000502:physiology*; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry; D011188:Potassium / Q000737:chemistry; D015221:Potassium Channels / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry
D008024:Ligands; D008565:Membrane Proteins; D010455:Peptides; D015221:Potassium Channels; D011506:Proteins; D011188:Potassium