A
postdoctoral position, funded primarily by an NIH grant, is available
immediately to study by NMR the solution structure and inter-component
interactions in pyruvate dehydrogenase and related multienzyme
complexes from different sources. The complexes are important in
metabolism and are excellent models for biological regulation as well.
The suitability of solution state NMR for their study has been
established. The group has more than 30 years of experience with
thiamin enzymes with active collaborations in both solution and solid
state NMR spectroscopy. The laboratory is located in the New York
metropolitan area, an outstanding environment for research.
Preference will be given to candidates with
demonstrated expertise in biomolecular, triple-resonance NMR,
especially the complete assignments and the solution structure
determination of large proteins. Experience and interest in enzymology,
molecular biophysics, and protein preparation and purification are
welcome. The project is on track to yield information not available by
x-ray structural studies to date. The candidate will be the major user
of an in-house Varian Inova 600 MHz spectrometer and will have access
to an 800 MHz NMR instrument as needed.
Please send inquiries, applications, and two to
three letters of recommendation to Professor Frank Jordan at frjordan@rutgers.edu
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