volume 141, issue 1-2, P30-47 2006
DOI: 10.1016/j.chemphyslip.2006.02.004
View full text
|
Sign up to set email alerts
|
Share

Abstract: AbstractThe folding mechanism of outer membrane proteins (OMPs) of Gram-negative bacteria into lipid bilayers has been studied using OmpA of E. coli and FomA of F. nucleatum as examples. Both, OmpA and FomA are soluble in unfolded form in urea and insert and fold into phospholipid bilayers upon strong dilution of the denaturant urea. OmpA is a structural protein and forms a small ion channel, composed of an 8-stranded transmembrane ␤-barrel domain. FomA is a voltage-dependent porin, predicted to form a 14 str…

Expand abstract

Search citation statements

Order By: Relevance

Citation Types

5
56
0

Paper Sections

0
0
0
0
0

Publication Types

0
0
0
0

Relationship

0
0

Authors

Journals