[RASMB] Postdoctoral Positions-Enzymology and Biochemistry of Blood Coagulation
Sriram Krishnaswamy
SKrishna at mail.med.upenn.edu
Thu Oct 27 06:48:44 PDT 2005
Dear Colleagues,
I have a couple of open postdoctoral positions in my laboratory.
Details are provided below.
Thanks.
Krishnaswamy
Sriram Krishnaswamy
Joseph Stokes Research Institute
Children's Hospital of Philadelphia
310A Abramson
3516 Civic Center Blvd
Philadelphia, PA 19104
Voice: (215) 590-3346
Fax: (215) 590-2320
E-mail: SKrishna at mail.med.upenn.edu
Postdoctoral positions are available to investigate the enzymology and
physical biochemistry of the membrane-dependent proteolytic reactions of
blood coagulation. The major areas of interest in the laboratory relate to
the specificity and function of the enzyme complex (prothrombinase) that
catalyses thrombin formation and the regulation of the initiation of
coagulation by the extrinsic Xase complex. These positions provide an
opportunity to be trained and make contributions in protein chemistry,
molecular biology/protein expression, thermodynamic measurements using
steady state fluorescence and isothermal titration calorimetry and kinetic
measurements including fluorescence stopped flow, rapid chemical quench and
time-resolved fluorescence spectroscopy.
The successful candidate is expected to have a Ph.D. in Biochemistry or
related discipline with a strong interest in protein chemistry, enzymology,
physical biochemistry and/or macromolecular interactions.
Those interested should send a CV with contact information for three
referees to:
Sriram Krishnaswamy
Joseph Stokes Research Institute
Children's Hospital of Philadelphia
and the University of Pennsylvania
310 Abramson, 3615 Civic Center Boulevard
Philadelphia, PA 19104
Voice: (215) 590-3346 Fax: (215) 590-2320 E-mail:
<mailto:Skrishna at mail.med.upenn.edu> Skrishna at mail.med.upenn.edu
Recent Publications:
Lu, G., Broze, J.G. and Krishnaswamy, S. (2004) Formation of Factors IXa and
Xa by the extrinsic pathway: Differential regulation by tissue factor
pathway inhibitor and antithrombin III. J. Biol. Chem. 279, 17241-17249.
Boskovic, D.S., Troxler, T. and Krishnaswamy, S. (2004) Active
Site-Independent Recognition of Substrates and Product by Prothrombinase. A
Fluorescence Resonance Energy Transfer Study. J. Biol. Chem. 279,
20786-20793.
Orcutt, S.J. and Krishnaswamy, S. (2004) Binding of substrate in two
conformations to human prothrombinase drives consecutive cleavage at two
sites in prothrombin. J. Biol. Chem., 279, 54927-54936
Lu, G., Chhum, S. and Krishnaswamy, S. (2005) The affinity of protein C for
the thrombin-thrombomodulin complex is determined in a primary way by active
site-dependent interactions J. Biol. Chem. 280, 15471-15478
Bianchini, E.P., Orcutt, S.J., Panizzi, P., Bock, P.E. and Krishnaswamy, S.
(2005) Ratcheting of the Substrate from the Zymogen to Proteinase
Conformations Directs Sequential Cleavage of Prothrombin by Prothrombinase
Proc. Natl. Acad. Sci. U.S.A. 102, 10099-10104
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