Manzi, L., Barrow, A. S., Hopper, J. T. S., Kaminska, R., Kleanthous, C., Robinson, C. V., Moses, J. E., Oldham, N. J. (November 2017) Carbene Footprinting Reveals Binding Interfaces of a Multimeric Membrane-Spanning Protein. Angew Chem Int Ed Engl, 56 (47). pp. 14873-14877. ISSN 1433-7851
Abstract
Mapping the interaction sites between membrane-spanning proteins is a key challenge in structural biology. In this study a carbene-footprinting approach was developed and applied to identify the interfacial sites of a trimeric, integral membrane protein, OmpF, solubilised in micelles. The diazirine-based footprinting probe is effectively sequestered by, and incorporated into, the micelles, thus leading to efficient labelling of the membrane-spanning regions of the protein upon irradiation at 349�nm. Areas associated with protein-protein interactions between the trimer subunits remained unlabelled, thus revealing their location.
Item Type: | Paper |
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Additional Information: | Angewandte Chemie (International ed. in English) |
CSHL Authors: | |
Communities: | CSHL labs > Moses lab |
Depositing User: | Matthew Dunn |
Date: | 20 November 2017 |
Date Deposited: | 08 Jan 2021 17:26 |
Last Modified: | 08 Jan 2021 17:26 |
URI: | https://repository.cshl.edu/id/eprint/39574 |
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