Lateral mobility of proteins in liquid membranes revisited

被引:306
作者
Gambin, Y
Lopez-Esparza, R
Reffay, M
Sierecki, E
Gov, NS
Genest, M
Hodges, RS
Urbach, W
机构
[1] Univ Paris 06, Ecole Normale Super, CNRS, Lab Phys Stat,Unite Mixte Rech 8550, F-75005 Paris, France
[2] Univ Paris 05, CNRS, Unite Mixte Rech 8638, F-75006 Paris, France
[3] Weizmann Inst Sci, Dept Phys Chem, IL-76100 Rehovot, Israel
[4] Univ Colorado, Dept Biochem & Mol Genet, Aurora, CO 80045 USA
关键词
bilayers; transmembrane proteins; diffusion; peptides; sponge phase;
D O I
10.1073/pnas.0511026103
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The biological function of transmembrane proteins is closely related to their insertion, which has most often been studied through their lateral mobility. For > 30 years, it has been thought that hardly any information on the size of the diffusing object can be extracted from such experiments. Indeed, the hydrodynamic model developed by Saffman and Delbruck predicts a weak, logarithmic dependence of the diffusion coefficient D with the radius R of the protein. Despite widespread use, its validity has never been thoroughly investigated. To check this model, we measured the diffusion coefficients of various peptides and transmembrane proteins, incorporated into giant unilamellar vesicles of 1-stearoyl-2-oleoylsn-glycero-3-phosphocholine (SOPC) or in model bilayers of tunable thickness. We show in this work that, for several integral proteins spanning a large range of sizes, the diffusion coefficient is strongly linked to the protein dimensions. A heuristic model results in a Stokes-like expression for D, (D proportional to 1/R), which fits literature data as well as ours. Diffusion measurement is then a fast and fruitful method; it allows determining the oligomerization degree of proteins or studying lipid-protein and protein-protein interactions within bilayers.
引用
收藏
页码:2098 / 2102
页数:5
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