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...

Πλήρης περιγραφή

Λεπτομέρειες βιβλιογραφικής εγγραφής
Κύριοι συγγραφείς:	Marcoux, J, Politis, A, Rinehart, D, Marshall, D, Wallace, M, Tamm, L, Robinson, C
Μορφή:	Journal article
Γλώσσα:	English
Έκδοση:	Cell Press 2014

Mass spectrometry defines the C-terminal dimerization domain and enables modeling of the structure of full-length OmpA. ανά Marcoux, J, Politis, A, Rinehart, D, Marshall, D, Wallace, M, Tamm, L, Robinson, C

Έκδοση 2014

Journal article

Mass spectrometry defines the C-terminal dimerization domain and enables modeling of the structure of full-length OmpA

Mass spectrometry defines the C-terminal dimerization domain and enables modeling of the structure of full-length OmpA. ανά Marcoux, J, Politis, A, Rinehart, D, Marshall, D, Wallace, M, Tamm, L, Robinson, C

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