Structural studies on membrane proteins using non-linear spin label EPR spectroscopy.
Non-linear electron spin resonance (EPR) techniques suitable for measuring proximity relationships in membranes are reviewed. These were developed during the past decade in order to measure changes sensitively in the spin-lattice relaxation time (T1) of nitroxyl spin labels covalently attached to membrane lipids or proteins. In combination with paramagnetic quenching agents and double spin-labelling, the methods were further developed for distance measurements. Selected examples are given to illustrate different methods, and types of data obtained for both integral and peripheral membrane proteins.
Páli
Tibor
T
Institute of Biophysics, Biological Research Centre, P.O.Box 521, 6701 Szeged, Hungary. tpali@nucleus.szbk.u-szeged.hu
Marsh
Derek
D
D004578:Electron Spin Resonance Spectroscopy / Q000379:methods*; D008563:Membrane Lipids / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry*; D017711:Nonlinear Dynamics; D011487:Protein Conformation; D013113:Spin Labels
D008563:Membrane Lipids; D008565:Membrane Proteins; D013113:Spin Labels