Mass spectrometry defines the C-terminal dimerization domain and enables modeling of the structure of full-length OmpA
The transmembrane domain of the outer membrane protein A (OmpA) from Escherichia coli is an excellent model for structural and folding studies of β-barrel membrane proteins. However, full-length OmpA resists crystallographic efforts, and the link between its function and tertiary structure remains c...
Huvudupphovsmän: | Marcoux, J, Politis, A, Rinehart, D, Marshall, D, Wallace, M, Tamm, L, Robinson, C |
---|---|
Materialtyp: | Journal article |
Språk: | English |
Publicerad: |
Cell Press
2014
|
Liknande verk
Liknande verk
-
Mass spectrometry defines the C-terminal dimerization domain and enables modeling of the structure of full-length OmpA.
av: Marcoux, J, et al.
Publicerad: (2014) -
Defining the function of OmpA in the Rcs stress response
av: Kilian Dekoninck, et al.
Publicerad: (2020-09-01) -
Role of OmpA1 and OmpA2 in Aggregatibacter actinomycetemcomitans and Aggregatibacter aphrophilus serum resistance
av: Mark Lindholm, et al.
Publicerad: (2019-01-01) -
Sequence and immunologic conservation of Anaplasma marginale OmpA within strains from Ghana as compared to the predominant OmpA variant.
av: James E Futse, et al.
Publicerad: (2019-01-01) -
Genotyping markers used for multi locus VNTR analysis with ompA (MLVA-ompA) and multi sequence typing retain stability in Chlamydia trachomatis
av: Clare eLabiran, et al.
Publicerad: (2012-05-01)