NSF Award
0923536
Post-translational modifications of proteins play a key role in the regulation of physiology and development. For example, reversible phosphorylation is the most common mechanism for cellular regulation in eukaryotic systems where it is estimated that roughly one third of the total protein complement of a cell is involved in this process. Coupled to this, the dynamic interactions of protein-protein and protein-DNA interactions provide a complex series of transient interactions crucial to life. In order to identify and measure all of these events in a systems biology approach, new mass spectrometry equipment and techniques must be developed. The development of high-Field Asymmetric waveform Ion Mobility Spectrometry to exploit the full potential of Electron Transfer Dissociation of peptides will provide steps towards more extensive measurement of these proteins. This project will not only enhance the research infrastructure at ISB but also integrate both educational activities and research goals to enhance the teaching, training and learning by providing innovative tools to maintain the cutting edge curriculum of courses held by ISB. Used by experimentalists and computational biologists, the data collected will ultimately inform researchers of proteome dynamics that are responsible for an organism's form and functions. Information derived from this development will be publicly accessible through the Seattle Proteome website (http://www.proteomecenter.org) as well as regular research publications.
