All Outputs (2)

Carbene Footprinting Reveals Binding Interfaces of a Multimeric Membrane-Spanning Protein (2017)
Journal Article
Manzi, L., Barrow, A. S., Hopper, J. T., Kaminska, R., Kleanthous, C., Robinson, C. V., Moses, J. E., & Oldham, N. J. (2017). Carbene Footprinting Reveals Binding Interfaces of a Multimeric Membrane-Spanning Protein. Angewandte Chemie International Edition, 56(47), 14873-14877. https://doi.org/10.1002/anie.201708254

© 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 in... Read More about Carbene Footprinting Reveals Binding Interfaces of a Multimeric Membrane-Spanning Protein.

A front-face 'SNi synthase' engineered from a retaining 'double-SN2' hydrolase (2017)
Journal Article
Iglesias-Fernández, J., Hancock, S. M., Lee, S. S., Khan, M., Kirkpatrick, J., Oldham, N. J., McAuley, K., Fordham-Skelton, A., Rovira, C., & Davis, B. G. (2017). A front-face 'SNi synthase' engineered from a retaining 'double-SN2' hydrolase. Nature Chemical Biology, 13, 874-881. https://doi.org/10.1038/nchembio.2394

SNi or SNi-like mechanisms, in which leaving group departure and nucleophile approach occur on the same ‘front’ face, have been observed previously experimentally and computationally in both the chemical and enzymatic (glycosyltransferase) substituti... Read More about A front-face 'SNi synthase' engineered from a retaining 'double-SN2' hydrolase.