期刊
JOURNAL OF CHEMICAL THEORY AND COMPUTATION
卷 15, 期 4, 页码 2608-2619出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jctc.8b01059
关键词
-
资金
- EPSRC [EP/L015722/1, EP/P020194/1]
- BBSRC [BB/H000658/1] Funding Source: UKRI
- EPSRC [EP/P020194/1, EP/R029407/1] Funding Source: UKRI
The outer membrane of Gram-negative bacteria has a highly complex asymmetrical architecture, containing a mixture of phospholipids in the inner leaflet and almost exclusively lipopolysaccharide (LPS) molecules in the outer leaflet. In E. coli, the outer membrane contains a wide range of proteins with a beta barrel architecture, that vary in size from the smallest having eight strands to larger barrels composed of 22 strands. Here we report coarse-grained molecular dynamics simulations of six proteins from the E. coli outer membrane OmpA, OmpX, BtuB, FhuA, OmpF, and EstA in a range of membrane environments, which are representative of the in vivo conditions for different strains of E. coli. We show that each protein has a unique pattern of interaction with the surrounding membrane, which is influenced by the composition of the protein, the level of LPS in the outer leaflet, and the differing mobilities of the lipids in the two leaflets of the membrane. Overall we present analyses from over 200 mu s of simulation for each protein.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据