Carbene Footprinting Reveals Binding Interfaces of a Multimeric Membrane-Spanning Protein

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

URL: https://pubmed.ncbi.nlm.nih.gov/28960650/
DOI: 10.1002/anie.201708254

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
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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