Structure determination of membrane-associated proteins from nuclear magnetic resonance data.
This Review covers the delineation and optimization of protein-lipid systems for study using solution-state NMR spectroscopy. The first half presents the necessary background for a membrane protein biochemist to initiate collaboration with an NMR spectroscopist. The second half provides guidelines for the spectroscopist on data collection, analysis for obtaining conformational information, and structure generation and assessment. Although the emphasis is on the study of peptides in detergent micelles, methods are outlined for larger membrane-associated proteins and for use of other solubilizing agents.
Baleja
J D
JD
Department of Biochemistry, Tufts University School of Medicine, 136 Harrison Avenue, Boston, Massachusetts, 02111, USA.
D003625:Data Collection; D003902:Detergents / Q000737:chemistry / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008563:Membrane Lipids / Q000737:chemistry / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D008823:Micelles; D017434:Protein Structure, Tertiary
D003902:Detergents; D008563:Membrane Lipids; D008565:Membrane Proteins; D008823:Micelles