Lipid‐protein interactions in membranes

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Abstract
The interactions of lipids with integral and peripheral proteins can be studied in reconstituted and natural membranes using spin label electron spin resonance (ESR) spectroscopy. The ESR spectra reveal a reduction in mobility of the spin‐labelled lipid chains on binding of peripheral proteins to negatively‐charged lipid bilayers. A selectivity of interaction has been established for different lipid species, and in certain cases evidence is obtained for a partial penetration of the peripheral proteins into the membrane. The latter may be relevant to the import mechanism of apocytochrome c into mitochondria. Integral proteins induce a more direct motional restriction of the spin‐labelled lipid chains, allowing the stoichiometry and specificity of the interaction, and the lipid exchange rate at the protein interface to be determined from the ESR spectra. In this way, a population of very slowly exchanging cardiolipin associated with the mitochondrial ADP‐ATP carrier has been identified. The residues involved in the specificity for charged lipids of the myelin proteolipid protein have been localized to the deletion in the DM‐20 mutant, and the difference in lipid‐protein interactions with the β‐sheet and α‐helical conformations of the M‐13 coat protein, has been characterized.

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