Stephen Kent (chemist)

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Stephen B. H. Kent (December 12, 1945 in Wellington, New Zealand) is a chemist at the University of Chicago and was a key developer of native chemical ligation along with Dr. Philip Dawson while professor at the Scripps Research Institute in the early 1990s.[1] He also demonstrated the principle that mirror-image amino acids put together to form a protein create a mirror-image protein which, if an enzyme, can catalyze the mirror-image reaction.[2] Currently, among a multitude of things, he is studying protein racemic crystallography.[3]

Biography[edit]

Dr. Kent was awarded a Ph.D. in chemistry from the University of California at Berkeley in 1975 following obtaining his M.Sc. at Massey University, Palmerston North, New Zealand in 1970 and bachelor degree in 1968.

Following his post-doctoral work in the laboratory of Dr. R. B. Merrifield at the Rockefeller University, Dr. Kent continued research there as an assistant professor until 1981. He has also held faculty positions at the California Institute of Technology, Bond University in Australia, and the Scripps Research Institute in California. Currently Dr. Kent is a professor in the Departments of Biochemistry & Molecular Biology and Chemistry at the University of Chicago. He is also the director for the Institute for Biophysical Dynamics. In addition to his academic achievements, he is the founder of two San Francisco Bay Area companies: Ciphergen Biosytems and Gryphon Therapeutics.

Dr. Kent has received numerous awards for his outstanding research. He was elected Fellow of the American Association for the Advancement of Science in 2000. He also received the Hirschmann Award in Peptide Chemistry from the American Chemical Society in 1994, the Kaiser Award from the Protein Society in 2002, and the 2009 Merrifield award from the American Peptide Society.

References[edit]

  1. ^ Synthesis of native proteins by chemical ligation. Dawson PE, Kent SB. Annu Rev Biochem. 2000;69:923-60.
  2. ^ Total chemical synthesis of a D-enzyme: the enantiomers of HIV-1 protease show reciprocal chiral substrate specificity [corrected]. Milton RC, Milton SC, Kent SB. Science. 1992 Jun 5;256(5062):1445-8
  3. ^ Chemical synthesis and X-ray structure of a heterochiral {D-protein antagonist plus vascular endothelial growth factor} protein complex by racemic crystallography. Mandal K, Uppalapati M, Ault-Riché D, Kenney J, Lowitz J, Sidhu SS, Kent SB. Proc Natl Acad Sci U S A. 2012 Sep 11;109(37):14779-84.

External links[edit]