Lipid‐protein interactions in membranes

FEBS Letters

Marsh, Derek¹ 

[1] Max-Planck-Institut für biophysikalische Chemie, Abt. Spektroskopie, D-3400 Göttingen, FRG

关键词: Integral protein;    Peripheral protein;    Lipid-protein interaction;    Spin label;    Electron spin resonance;   

DOI  :  10.1016/0014-5793(90)81288-Y

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown