Saturation Transfer EPR Studies of Rotational Dynamics in Membranes
Beginning about 10 years ago, electron paramagnetic resonance (EPR) studies on spinlabeled lipids, pioneered by McConnell and co-workers, have helped elucidate the dynamic properties of the lipid components of both synthetic and biological membranes. While the conventional EPR technique is ideally suited to monitor the nanosecond rotational motions of fluid lipid hydrocarbon chains or small protein segments, that technique is insensitive to the slower motions (often in the microsecond range) that are typical for gel-phase lipid and entire membrane proteins. In contrast, saturation transfer EPR (ST-EPR), a technique introduced by Hyde and Dalton (1972), has its optimum sensitivity in the microsecond region (recent reviews: Thomas, 1978; Hyde and Dalton, 1979; Hyde and Thomas, 1980). Since the introduction of the ST-EPR capability in commercial spectrometers about 4 years ago, this technique has proven to be a powerful tool in the study of membrane dynamics, particularly the rotational motions of integral membrane proteins.
KeywordsElectron Paramagnetic Resonance Spin Label Integral Membrane Protein Rotational Dynamics Nitroxide Group
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