Stephen B.H. Kent
Research Summary / Selected Publications
We apply the tools of chemistry to elucidate the molecular basis of the biological functions of proteins. Ultimately we want to be able to design and build protein molecules with pre-determined, controlled properties. This is a scientific problem of great timeliness with the completion of the genome sequencing projects, which impact broadly across the natural sciences.
In the post-genome era it will be imperative to understand the principles that govern the numerous and diverse activities of proteins in the biological world. These principles can best be elucidated by combining a number of scientific disciplines. To that end, we have established general synthetic access to the world of proteins. This enables us to focus the most advanced physical and chemical techniques in conjunction with all the tools of molecular biology to elucidate the molecular basis of the biochemical and biological actions of the protein molecule.
The emphasis in our research program is on collaborative science. This creates unique opportunities for people drawn to the application of chemistry to biological systems. Thus, techniques such as Xray crystallography, nuclear magnetic resonance (NMR), and Fourier-transform infrared (FTIR) spectroscopy...
A one-pot approach to neoglycopeptides using orthogonal native chemical ligation and click chemistry.
Dong Jun Lee, Kalyaneswar Mandal, Paul W. R. Harris, Margaret A. Brimble, Stephen B. H. Kent.
Organic Letters, 11, 5270-3 (2009).
Total chemical synthesis and racemic protein crystallography used to determine the X-ray structure of plectasin by direct methods.
Kalyaneswar Mandal, Brad L. Pentelute, Valentina Tereshko, Anthony A. Kossiakoff, Stephen B. H. Kent,
18, 1146-1154 (2009). Cover
Dynamics of ‘flap’ structures in three HIV-1 protease/inhibitor complexes probed by total chemical synthesis and pulse-EPR spectroscopy.
Vladimir Yu. Torbeev, Kalyaneswar Mandal, Sanjib Senapati, Eduardo Perozo, Stephen B. H. Kent,
J Am Chem Soc,
131, 884-5 (2009).
Crystal structure of chemically synthesized HIV-1 protease and a ketomethylene isostere inhibitor based on the p2/NC cleavage site.
V. Yu. Torbeev, K. Mandal, V. A. Terechko, S. B. H. Kent,
Bioorganic & Medicinal Chemistry Letters, 18, 4554-7 (2008).