Abstract

Twelve NIH supported investigators request funds to purchase a high sensitivity ion trap mass spectrometer system, including two dimensional LC, electro spray ionization, data dependent acquisition, and protein/peptide identification and measurement software. The instrument will generate peptide sequence information for protein identification and for locating sites of posttranslational modification, and quantitative data for proteome characterization as a function of cell state for four major users and eight minor users. The instrument will be located in the Laboratory for Bioanalysis and Biotechnology, Unit 2, WSU's core MS facility. Research projects to be supported by this instrument include identifying proteins/peptides associated with sleep responses in a mutant strain of mouse, gene expression in somatic and germ cells during spermatogenesis, primordial follicle development, cell-cell interactions and testis development, and the role of titin's kinase domain in muscle function and disease. ? ?

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biomedical Research Support Shared Instrumentation Grants (S10)
Project #
1S10RR017805-01
Application #
6580482
Study Section
Special Emphasis Panel (ZRG1-BECM (02))
Program Officer
Tingle, Marjorie
Project Start
2003-05-01
Project End
2004-04-30
Budget Start
2003-05-01
Budget End
2004-04-30
Support Year
1
Fiscal Year
2003
Total Cost
$327,673
Indirect Cost

  Institution

Name
Washington State University
Department
Biology
Type
Schools of Arts and Sciences
DUNS #
041485301
City
Pullman
State
WA
Country
United States
Zip Code
99164

  Publications

Chowdhury, Saiful M; Munske, Gerhard R; Yang, Jonathon et al. (2014) Solid-phase N-terminal peptide enrichment study by optimizing trypsin proteolysis on homoarginine-modified proteins by mass spectrometry. Rapid Commun Mass Spectrom 28:635-44
Zhang, Haizhen; Tang, Xiaoting; Munske, Gerhard R et al. (2009) Identification of protein-protein interactions and topologies in living cells with chemical cross-linking and mass spectrometry. Mol Cell Proteomics 8:409-20
Yang, Li; Zhang, Haizhen; Bruce, James E (2009) Optimizing the detergent concentration conditions for immunoprecipitation (IP) coupled with LC-MS/MS identification of interacting proteins. Analyst 134:755-62
Noh, Susan M; Brayton, Kelly A; Brown, Wendy C et al. (2008) Composition of the surface proteome of Anaplasma marginale and its role in protective immunity induced by outer membrane immunization. Infect Immun 76:2219-26
Zhang, Haizhen; Tang, Xiaoting; Munske, Gerhard R et al. (2008) In vivo identification of the outer membrane protein OmcA-MtrC interaction network in Shewanella oneidensis MR-1 cells using novel hydrophobic chemical cross-linkers. J Proteome Res 7:1712-20
Wu, Si; Tang, Xiao-Ting; Siems, William F et al. (2005) A hybrid LC-Gel-MS method for proteomics research and its application to protease functional pathway mapping. J Chromatogr B Analyt Technol Biomed Life Sci 822:98-111
Chowdhury, Saiful M; Munske, Gerhard R; Siems, William F et al. (2005) A new maleimide-bound acid-cleavable solid-support reagent for profiling phosphorylation. Rapid Commun Mass Spectrom 19:899-909
Tang, Xiaoting; Munske, Gerhard R; Siems, William F et al. (2005) Mass spectrometry identifiable cross-linking strategy for studying protein-protein interactions. Anal Chem 77:311-8