A total of 10 investigators with 19 NIH-funded projects constituting major users and 4 other-funded investigators representing minor users request funds to support purchase of an LC-LTQ-FT mass spectrometer. This instrument will be sited in the WSU Proteomics and Mass Spectrometry Core Facility that currently supports research over 50 faculty members in more than 10 different departments. Among other unique features, the LTQ-FT provides routine unparalleled high mass measurement accuracy LC/MS/MS capabilities. High mass measurement accuracy is the most constraining search criterion in both proteome and metabolome component identification. In addition, LTQ-FT has high speed MS/MS, automatic data-dependent MS2 and MS3, ECD and/or IRMPD during LC separation that will enable improved metabolite and protein identification, increased post-translational modification mapping, and enhanced crosslinked peptide identification for protein-protein interaction studies. These outstanding capabilities of the LTQ-FT will benefit all projects in WSU, such as the characterization of metabolomic and proteomic changes relevant to cancer, quantitative proteome and post-translational modification changes related to reproductive biology, and quantitative proteomics and protein interactions involved in immune response. Data generated using this new instrument will significantly enable success of this large group of NIH-funded investigators.

Public Health Relevance

The relevance of this requested instrumentation can be categorized primarily into three broad areas of human health research: 1) cancer biology, 2) reproductive biology, and 3) immunology. All three areas are the focus of significant proteomics and metabolomics research aimed at improvement of overall human health, prevention and treatment of disease. The relevance of this application toward achieving those goals is based on the significantly improved and unique capabilities the requested instrumentation will bring to bear on protein, posttranslational modification, protein-protein interaction, and metabolite quantitation and identification. ? ? ?

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biomedical Research Support Shared Instrumentation Grants (S10)
Project #
7S10RR025107-02
Application #
7760288
Study Section
Special Emphasis Panel (ZRG1-BCMB-M (30))
Program Officer
Tingle, Marjorie
Project Start
2008-07-01
Project End
2010-06-30
Budget Start
2008-12-06
Budget End
2010-06-30
Support Year
2
Fiscal Year
2008
Total Cost
$989,825
Indirect Cost
Name
University of Washington
Department
Genetics
Type
Schools of Medicine
DUNS #
605799469
City
Seattle
State
WA
Country
United States
Zip Code
98195
Zhong, Xuefei; Navare, Arti T; Chavez, Juan D et al. (2017) Large-Scale and Targeted Quantitative Cross-Linking MS Using Isotope-Labeled Protein Interaction Reporter (PIR) Cross-Linkers. J Proteome Res 16:720-727
Schweppe, Devin K; Chavez, Juan D; Lee, Chi Fung et al. (2017) Mitochondrial protein interactome elucidated by chemical cross-linking mass spectrometry. Proc Natl Acad Sci U S A 114:1732-1737
Chavez, Juan D; Schweppe, Devin K; Eng, Jimmy K et al. (2016) In Vivo Conformational Dynamics of Hsp90 and Its Interactors. Cell Chem Biol 23:716-26
Chavez, Juan D; Eng, Jimmy K; Schweppe, Devin K et al. (2016) A General Method for Targeted Quantitative Cross-Linking Mass Spectrometry. PLoS One 11:e0167547
Wu, Xia; Chavez, Juan D; Schweppe, Devin K et al. (2016) In vivo protein interaction network analysis reveals porin-localized antibiotic inactivation in Acinetobacter baumannii strain AB5075. Nat Commun 7:13414
Wu, Xia; Held, Kiara; Zheng, Chunxiang et al. (2015) Dynamic Proteome Response of Pseudomonas aeruginosa to Tobramycin Antibiotic Treatment. Mol Cell Proteomics 14:2126-37
Navare, Arti T; Chavez, Juan D; Zheng, Chunxiang et al. (2015) Probing the protein interaction network of Pseudomonas aeruginosa cells by chemical cross-linking mass spectrometry. Structure 23:762-73
Chavez, Juan D; Schweppe, Devin K; Eng, Jimmy K et al. (2015) Quantitative interactome analysis reveals a chemoresistant edgotype. Nat Commun 6:7928
Vaitheesvaran, B; Hartil, K; Navare, A et al. (2014) Role of the tumor suppressor IQGAP2 in metabolic homeostasis: Possible link between diabetes and cancer. Metabolomics 10:920-937
Weisbrod, Chad R; Hoopmann, Michael R; Senko, Michael W et al. (2013) Performance evaluation of a dual linear ion trap-Fourier transform ion cyclotron resonance mass spectrometer for proteomics research. J Proteomics 88:109-19

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