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Mass Spectrometry and Proteomics - Correlating Structure with Function

presented by

Jeffrey J. Gorman
CSIRO / Biomolecular Research Institute

August 21, 2002

The Scripps Research Institute, W.M. Keck Foundation Amphitheater


Background:

Dr. Gorman received both his B.S. in Chemistry and Biochemistry and his Ph.D in Biochemistry from the University of Melbourne. He is currently the Senior Principal Research Scientist at CSIRO/Biomolecular Research Institute in Melbourne, Australia.

Abstract:

Mass spectrometry is the key technology underpinning the exploitation of genomic sequence databases using proteomics approaches. Using MALDI-TOF-MS and nanoElectrospray-QTOF-MS/MS, it is possible to get mass and sequencing information on minute quantities of peptides and to determine the existence and characteristics of post-translational modifications. This presentation will involve studies that have defined the disulfide bonds and glycosylation of paramyxovirus membrane glycoproteins. This will include use of oxygen (18) incorporation during proteolysis as a means of identifying and characterizing disulfide-linked peptides. Identification of asparagine hydroxylation of hypoxia inducible factor (HIF) as a trascriptional switch in response to cellular oxygen status, will also be described. This study involved combined use of MALDI-TOF-MS and nanoElectrospray-QTOF-MS/MS of the HIF C-terminal transactivation domain after expression in cells under hypoxic and normoxic conditions. A similar approach has also been used to characterize the enzyme that catalyses the asparagine hydroxylation.

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