Biophysical approaches to membrane protein structure determination.
Recently, there have been several technical advances in the use of solution and solid-state NMR spectroscopy to determine the structures of membrane proteins. The structures of several isolated transmembrane (TM) helices and pairs of TM helices have been solved by solution NMR methods. Similarly, the complete folds of two TM beta-barrel proteins with molecular weights of 16 and 19 kDa have been determined by solution NMR in detergent micelles. Solution NMR has also provided a first glimpse at the dynamics of an integral membrane protein. Structures of individual TM helices have also been determined by solid-state NMR. A combination of NMR with site-directed spin-label electron paramagnetic resonance or Fourier transform IR spectroscopy allows one to assemble quite detailed protein structures in the membrane.
Arora
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Department of Molecular Physiology and Biological Physics, and Center for Structural Biology, University of Virginia, Health System, Charlottesville 22908-0736, USA.
Tamm
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D001703:Biophysics / Q000379:methods*; D004578:Electron Spin Resonance Spectroscopy; D008051:Lipid Bilayers; D008565:Membrane Proteins / Q000737:chemistry*; D008823:Micelles; D008958:Models, Molecular; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D011487:Protein Conformation; D012996:Solutions; D017550:Spectroscopy, Fourier Transform Infrared; D013816:Thermodynamics
D008051:Lipid Bilayers; D008565:Membrane Proteins; D008823:Micelles; D012996:Solutions