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Kristina Hkansson of the University of Michigan, Ann Arbor, and Timothy J. Griffin of the University of Minnesota, Twin Cities, are the recipients of the annual Analytical Chemistry Grantee Award presented by the Analytical Chemistry Academic Contact Committee of Eli Lilly & Co. This award is presented to new professors who have quickly distinguished themselves as leaders in the field of analytical chemistry. It is an unsolicited, unrestricted grant funded at a level of $20,000 per year, renewable for a second year. Both awardees have a strong interest in developing novel techniques and applying mass spectrometry to solving biologically relevant problems.
Hkansson's research focuses on the use of state-of-the-art Fourier transform ICR (ion cyclotron resonance) mass spectrometry coupled with ECD (electron-capture dissociation), EDD (electron-detachment dissociation), IR MPD (multiphoton dissociation), H/D exchange, and other structurally informative techniques to determine nucleic acid structure and sequence, characterize protein posttranslational modifications, and map macromolecular contact surfaces.
The Hkansson lab is establishing the fragmentation pathways and mechanisms of ECD and EDD of oligonucleotides and oligosaccharides. The analytical utility of EDD is also being explored for the characterization of negatively charged phosphopeptides and glycopeptides.
Griffin's long-term goal is to develop tools that enable comprehensive characterization of the entire complement of proteins expressed within a cell, tissue, or organism. His research lab has developed the use of field-flow electrophoresis for isoelectric focusing of peptides in complex mixtures combined with tandem mass spectrometry as a tool for high-throughput proteomics.
Griffin's group is studying changes in the glycosylation state of proteins in saliva as a marker of oral cancer progression. In collaboration with two other University of Michigan groups, Griffin has developed a method to identify oxidized proteins to study the role of oxidative-stress-mediated carbonylation of the proteome of aging muscle mitochondria.
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