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 controversial. Here we use site-directed mutagenesis and mass spectrometry of different constructs of OmpA, released in the gas phase from detergent micelles, to define the minimal region encompassi...Expand abstract
- Publication status:
- Publisher copy:
- Copyright date:
Views and Downloads
If you are the owner of this record, you can report an update to it here: Report update to this record