title: The measurement of immersion depth and topology of membrane proteins by solution state NMR.
abstract: An important component of the study of membrane proteins involves the determination of details associated with protein topology - for example, the location of transmembrane residues, specifics of immersion depth, orientation of the protein in the membrane, and extent of solvent exposure for each residue. Solution state NMR is well suited to the determination of immersion depth with the use of paramagnetic additives designed to give rise to depth-specific relaxation effects or chemical shift perturbations. Such additives include spin labels designed to be "anchored" within a given region of the membrane or small freely diffusing paramagnetic species, whose partitioning properties across the water membrane interface create a gradient of paramagnetic effects which correlate with depth. This review highlights the use of oxygen and other small paramagnetic additives in studies of immersion depth and topology of membrane proteins in lipid bilayers and micelles.
authors.affiliation: Department of Chemistry, University of Toronto, UTM, 3359 Mississauga Rd. North, Mississauga, ON, Canada L5L 1C6. scott.prosser@utoronto.ca
authors.forename: R Scott
authors.initials: RS
authors.lastname: Prosser
authors.forename: Ferenc
authors.initials: F
authors.lastname: Evanics
authors.forename: Julianne L
authors.initials: JL
authors.lastname: Kitevski
authors.forename: Sagar
authors.initials: S
authors.lastname: Patel
mesh_terms: D008051:Lipid Bilayers / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008565:Membrane Proteins / Q000737:chemistry*; D012996:Solutions
chemical_list: D008051:Lipid Bilayers; D008565:Membrane Proteins; D012996:Solutions