@article { , title = {Carbene Footprinting Reveals Binding Interfaces of a Multimeric Membrane-Spanning Protein}, abstract = {© 2017 Wiley-VCH Verlag GmbH \& Co. KGaA, Weinheim. 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.}, doi = {10.1002/anie.201708254}, eissn = {1521-3773}, issn = {1433-7851}, issue = {47}, journal = {Angewandte Chemie - International Edition}, pages = {14873-14877}, publicationstatus = {Published}, publisher = {Wiley}, url = {https://nottingham-repository.worktribe.com/output/895876}, volume = {56}, keyword = {carbene footprinting, integral membrane proteins, mass spectrometry, protein labelling, protein structures}, year = {2017}, author = {Manzi, Lucio and Barrow, Andrew S. and Hopper, Jonathan T.S. and Kaminska, Renata and Kleanthous, Colin and Robinson, Carol V. and Moses, John E. and Oldham, Neil J.} }