Work

Membrane Lipids Influence Protein Complex Assembly−Disassembly

Year: 2010

Type: article

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.

Source: Journal of the American Chemical Society

DOI: 10.1021/ja101574d

Authors: Leah Shin, Won Jin Cho, Jeremy D. Cook, Timothy L. Stemmler, Bhanu P. Jena

Institution: Wayne State University

Language: English

Topic: Lipid Membrane Structure and Behavior

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Institutes of Health, National Institute of Diabetes and Digestive and Kidney Diseases, National Institute of Biomedical Imaging and Bioengineering

Awards: G5312588033, UNDERSTANDING MEMBRANE FUSION A BIOENGINEERING APPROACH, Structural Insights into the Function of Frataxin