Structural studies on membrane proteins using non-linear spin label EPR 
spectroscopy

Pali, T.; Marsh, D.

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Structural studies on membrane proteins using non-linear spin label EPR spectroscopy

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Pali, T.
Department of Spectroscopy and Photochemical Kinetics, MPI for biophysical chemistry, Max Planck Society;

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Marsh, D.
Department of Spectroscopy and Photochemical Kinetics, MPI for biophysical chemistry, Max Planck Society;

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Citation

Pali, T., & Marsh, D. (2002). Structural studies on membrane proteins using non-linear spin label EPR spectroscopy. Cellular & Molecular Biology Letters, 7(1), 87-91. Retrieved from http://www.cmbl.org.pl/pdf/Vol7_p087.pdf.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0012-F4AC-8

Abstract

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 (T-1) 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.