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...
Egile Nagusiak: | Marcoux, J, Politis, A, Rinehart, D, Marshall, D, Wallace, M, Tamm, L, Robinson, C |
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Formatua: | Journal article |
Hizkuntza: | English |
Argitaratua: |
Cell Press
2014
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