and Mass Spectrometry

Upcoming Speakers

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


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.


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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