title: Secondary structure of the outer membrane proteins OmpA of Escherichia coli and OprF of Pseudomonas aeruginosa.
abstract: 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.
authors.affiliation: Department of Molecular and Cell Biology, University of California, Berkeley, USA.
authors.forename: E
authors.initials: E
authors.lastname: Sugawara
authors.forename: M
authors.initials: M
authors.lastname: Steiert
authors.forename: S
authors.initials: S
authors.lastname: Rouhani
authors.forename: H
authors.initials: H
authors.lastname: Nikaido
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D002942:Circular Dichroism; D004926:Escherichia coli / Q000737:chemistry*; D006358:Hot Temperature; D018272:Porins / Q000737:chemistry*; D017433:Protein Structure, Secondary; D011550:Pseudomonas aeruginosa / Q000737:chemistry*
chemical_list: D001425:Bacterial Outer Membrane Proteins; D018272:Porins