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Membrane lipids influence protein complex assembly-disassembly.

ABSTRACT: 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 alpha-helical contents within the t-/v-SNARE complex.

SUBMITTER: Shin L

PROVIDER: S-EPMC2862647 | biostudies-literature | 2010 Apr

REPOSITORIES: biostudies-literature

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Membrane lipids influence protein complex assembly-disassembly.

Shin Leah L Cho Won Jin WJ Cook Jeremy D JD Stemmler Timothy L TL Jena Bhanu P BP

Journal of the American Chemical Society 20100401 16

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 alpha-helical contents within the t-/v-SNARE complex. ...[more]

PMID: 20373736

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