A postdoctoral position to study the solution dynamics and structure
of protein kinases is available on a NIH funded project (REF#:
HS-R-6453-10-08-S). Our group is interested in how static and dynamic
changes of protein structure affect the activity of protein kinases.
We combine X-ray crystallography, NMR and ligand binding kinetics with
collaborative molecular dynamic studies (See e.g. ref 1 and 2). Our
research group is located at Stony Brook University in a highly
interactive environment with the New York Structural Biology Center
and Brookhaven National Laboratory. Varian and Bruker NMR instruments
with 500-700 MHz field strenghts are available on site. As a member of
the New York Structural Biology Center, we have access to 800 MHz and
900 MHz instruments as well as a access to a large pool of NMR
expertise. The location of Stony Brook University within public
transport commuting distance to New York City and the north shore of
Long Island provide a convenient work-life balance and a family
friendly environment.
Interested candidates with a strong background in protein NMR should
email their CV and the names of three references to Markus Seeliger
(markus.seeliger@gmail.com).
1.) Shan, Y., Seeliger, M.A., et al. A conserved
protonation-dependent switch controls drug binding in the Abl kinase.
Proc Natl Acad Sci U S A, 2009. 106(1): p. 139-44.
2.) Seeliger, M.A., et al., Equally potent inhibition of c-Src and Abl
by compounds that recognize inactive kinase conformations. Cancer Res,
2009. 69(6): p. 2384-92.
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Markus Seelige
Assistant Professor
Department of Pharmacological Sciences
Stony Brook University Medical School, BST 7-125
Stony Brook, NY 11794-8651
phone: (631) 444-3558 fax: (631) 444-9749
http://www.pharm.stonybrook.edu/seeliger
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