Sugawara E, Steiert M, Rouhani S, Nikaido H
Department of Molecular and Cell Biology, University of California, Berkeley, USA.
J Bacteriol. 1996 Oct;178(20):6067-9. doi: 10.1128/jb.178.20.6067-6069.1996.
When purified without the use of ionic detergents, both OmpA and OprF proteins contained nearly 20% alpha-helical structures, which disappeared completely upon the addition of sodium dodecyl sulfate. This result suggests that the proteins fold in a similar manner, with an N-terminal, membrane-spanning beta-barrel domain and a C-terminal, globular, periplasmic domain.
在不使用离子去污剂的情况下进行纯化时，OmpA和OprF蛋白均含有近20%的α-螺旋结构，而在添加十二烷基硫酸钠后这些结构完全消失。这一结果表明，这些蛋白质以相似的方式折叠，具有一个N端跨膜β桶结构域和一个C端球状周质结构域。
