Models for the structure of outer-membrane proteins of Escherichia coli derived from Raman spectroscopy and prediction methods

The secondary structure of porin, maltoporin, and OmpA protein reconstituted in lipid membranes was detd. by Raman spectroscopy. The 3 proteins have similar structures consisting of 50-60% b-strand, .apprx.20% b-turn, and <15% a-helix. By using a method for structural prediction that accounts for amphipathic b-strands, folding models were developed for porin and for the segment of OmpA protein incorporated into the membrane. In the model, the OmpA fragment consists of 8 amphipathic membrane-spanning b-strands that form a b-barrel. Similarly, porin is folded into 10 amphipathic membrane-spanning b-strands that are located at the surface of the trimer towards the lipids and 8 predominantly hydrophilic strands in the interior. [on SciFinder (R)]


Published in:
Journal of Molecular Biology, 190, 2, 191-9
Year:
1986
Laboratories:




 Record created 2006-02-27, last modified 2018-03-17


Rate this document:

Rate this document:
1
2
3
 
(Not yet reviewed)