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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.

Original publication

DOI

10.1002/anie.201708254

Type

Journal article

Journal

Angewandte Chemie (International ed. in English)

Publication Date

11/2017

Volume

56

Pages

14873 - 14877

Addresses

School of Chemistry, University of Nottingham, University Park, Nottingham, NG7 2RD, UK.