Thermodynamics of glycophorin A transmembrane helix dimerization in C14 betaine micelles

被引：43

作者：

Fleming, KG ^{[1
]}

Ren, CC ^{[1
]}

Doura, AK ^{[1
]}

Eisley, ME ^{[1
]}

Kobus, FJ ^{[1
]}

Stanley, AM ^{[1
]}

机构：

[1] Johns Hopkins Univ, TC Jenkins Dept Biophys, Baltimore, MD 21218 USA

来源：

BIOPHYSICAL CHEMISTRY | 2004年 / 108卷 / 1-3期

关键词：

membrane protein; transmembrane interactions; interaction thermodynamics;

D O I：

10.1016/j.bpc.2003.10.008

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We have used sedimentation equilibrium analytical ultracentrifugation to measure the free energy change for the glycophorin A transmembrane helix-helix dimerization in C14 betaine micelles. By varying the amount of micellar C14 betaine, we show that the protein association reaction in the micellar C14 phase behaves as an ideal-dilute solution. In this hydrophobic environment, the mole-fraction standard state free energy change for self-association of the SNGpA99 glycophorin A construct is -5.7 (+/-0.3, N=5) kcal mol(-1) at 25 degreesC. Compared with previous results carried out in C8E5 micellar solutions, the free energy of dimerization is 1.3 kcal mol(-1) less favorable in C14 betaine micelles. In contrast, when considered on a per-interface basis, the formation of the glycophorin A transmembrane dimer in C14 betaine micelles may be more favorable than the association of several designed transmembrane peptides. (C) 2003 Elsevier B.V. All rights reserved.

引用

页码：43 / 49

页数：7

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