Linear Ion Trap for Proteomics

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DESCRIPTION (provided by applicant): The goal of this proposal is to bring a LTQ-11000 Linear Ion Trap Mass Spectrometer with 2D nan-LC to Wayne State University. This instrument, designed to perform peptide sequence analysis and to identify and localize post-translational modifications in proteins, will be a major asset to research programs of NIH-funded investigators at WSU whose research is focused primarily on the regulation of cellular signal transduction pathways in healthy and diseased states. It is well established that control of these pathways is dependent on protein interactions and regulated changes in enzyme activities, many of which are modulated by post- translation modifications. Primary Users of the proposed LTQ Linear Ion Trap Mass Spectrometer work on signaling pathways that are modulated by phosphorylation or oxidation. Their research requires identification of proteins and analysis of the post-translational modifications of those proteins in response to specific stimuli and/or in specific disease states. The only unequivocal way to address these questions is through mass spectrometry. There is no MS/MS instrument at Wayne State or in the metropolitan Detroit area that can be used for proteomic analysis. The Proteomics Facility Core within the EHS Center at WSU has been established as the first source for these proteomic services at Wayne State. The University is strongly committed to this proposal as evidenced by the following support: 1) A funded long term plan for maintenance and operation of the LTQ Linear Ion Trap MS. 2) Dedicated laboratory space for a Proteomic Core Facility that will house the instrument. 3) Funding for salary and training of a technician to operate and schedule usage of the instrument. The LTQ-11000 Linear Ion Trap Mass Spectrometer is a state-of-the-art system with unparalleled speed and the ability to detect and localize post-translational modifications in proteins. At WSU, this instrument will allow more productive use of instrumentation already in place for proteomic fractionation and will provide efficient access to modern proteomic analysis for NIH-funded investigators who are now limited by the lack of local proteomic support.