title: Customizing model membranes and samples for NMR spectroscopic studies of complex membrane proteins.
abstract: Both solution and solid state nuclear magnetic resonance (NMR) techniques for structural determination are advancing rapidly such that it is possible to contemplate bringing these techniques to bear upon integral membrane proteins having multiple transmembrane segments. This review outlines existing and emerging options for model membrane media for use in such studies and surveys the special considerations which must be taken into account when preparing larger membrane proteins for NMR spectroscopic studies.
authors.affiliation: Department of Physiology and Biophysics, Case Western Reserve University, 44106-4970, Cleveland, OH, USA. crs4@po.cwru.edu
authors.forename: C R
authors.initials: CR
authors.lastname: Sanders
authors.forename: K
authors.initials: K
authors.lastname: Oxenoid
mesh_terms: D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008565:Membrane Proteins / Q000737:chemistry*; D008567:Membranes, Artificial; D008823:Micelles; D008956:Models, Chemical; D017510:Protein Folding
chemical_list: D008565:Membrane Proteins; D008567:Membranes, Artificial; D008823:Micelles