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J. Bacteriol., Oct 1996, 6067-6069, Vol 178, No. 20
E Sugawara, M Steiert, S Rouhani and H Nikaido
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.
Copyright © 1996, American Society for Microbiology
Secondary structure of the outer membrane proteins OmpA of Escherichia coli and OprF of Pseudomonas aeruginosa
Department of Molecular and Cell Biology, University of California, Berkeley, USA.
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