Secondary structure of the outer membrane proteins OmpA of Escherichia coli and OprF of Pseudomonas aeruginosa.
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.
Sugawara
E
E
Department of Molecular and Cell Biology, University of California, Berkeley, USA.
Steiert
M
M
Rouhani
S
S
Nikaido
H
H
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*
D001425:Bacterial Outer Membrane Proteins; D018272:Porins