期刊
JOURNAL OF PHYSICAL CHEMISTRY B
卷 113, 期 3, 页码 589-591出版社
AMER CHEMICAL SOC
DOI: 10.1021/jp808776z
关键词
-
资金
- National Natural Science Foundation of China [20674093]
A dissipative particle dynamics simulation method is used to probe the mechanism of protein-mediated membrane fusion. The coarse-grained models for proteins are designed based on the function of fusion proteins. Attractive forces have been introduced to produce a protein complex. The formation of protein complexes provides mechanical forces to bring membranes in proximity and trigger their merging. The whole fusion process is in good agreement with the scaffold hypothesis. Additionally, if self-defined interactions are also imposed on transmembrane segments (TMSs), their association will yield an unstable fusion pore, which can incorporate lipid and water to accomplish membrane fusion. It indicates the formation of a protein-lined pore will promote the stalk-pore transition and accelerate the fusion process.
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