Membrane Lipids Influence Protein Complex Assembly-Disassembly

被引：18

作者：

Shin, Leah ^{[1
]}

Cho, Won Jin ^{[1
]}

Cook, Jeremy D. ^{[2
]}

Stemmler, Timothy L. ^{[2
]}

Jena, Bhanu P. ^{[1
]}

机构：

[1] Wayne State Univ, Sch Med, Dept Physiol, Detroit, MI 48201 USA

[2] Wayne State Univ, Sch Med, Dept Biochem & Mol Biol, Detroit, MI 48201 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2010年 / 132卷 / 16期

关键词：

SNARE COMPLEX; CURVATURE; FUSION; ENERGY;

D O I：

10.1021/ja101574d

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Approximately 11% smaller t-/v-SNARE ring complexes are generated using 50 nm cholesterol-associated vesicles as opposed to vesicles containing L-alpha-lysophosphatidylcholine (LPC), as observed using atomic force microscopy. Circular dichroism spectroscopy demonstrated that in the presence of LPC as opposed to cholesterol, N-ethylmaleimide-sensitive factor + adenosine triphosphate induces disassembly of beta-sheet structures but not the a-helical contents within the t-/v-SNARE complex.

引用

页码：5596 / +

页数：3

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