This subproject is one of many research subprojects utilizing the resources provided by a Shared Instrumentation Grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the grant, which is not necessarily the institution for the investigator. DESCRIPTION (provided by applicant): A total of 4 NIH investigators that constitute the major users and 2 other federally-funded investigators that represent minor users request funds to support purchase of a MALDI mass spectrometer with MS/MS capabilities and associated sample separations and sample preparation equipment. This instrument will be placed in the growing WSU Mass Spectrometry and Proteomics Core Facility and will more efficiently handle the large number of samples that are currently dependent on a 10 year old ABI Voyager MALDI-TOF that is becoming difficult to maintain due to availability of parts. In addition, this instrument will enable new capabilities for MS/MS analysis of MALDI-generated ions that is currently not possible at WSU. The requested instrument will dramatically expand the Core Lab abilities to provide peptide mass fingerprint and MS/MS-based protein identification information that is critical to many NIH-funded projects on the WSU campus and on the nearby University of Idaho campus. Specific NIH-funded projects outlined in this proposal that will constitute major users of the technology include, proteomics experiments to identify secreted proteins that mediate cell-cell interactions involved in testis development and primordial follicle development (Co-Pi Skinner), phosphoproteome profiling to study the regulation of retinoic acid receptor effects on testis development (Co-Pi Kim), protein-interaction studies to investigate molecular components of cellular motility (Co-Pi Cole) and proteomics investigations of immunoresponse relevant to Anaplasma maginalis (Co-Pi Brown). Large-scale proteomics research is becoming increasingly critical in these projects and in many others and the requested instrumentation enables the WSU Core Lab to support this research.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biomedical Research Support Shared Instrumentation Grants (S10)
Project #
1S10RR022538-01
Application #
7335236
Study Section
Special Emphasis Panel (ZRG1-BCMB-D (30))
Project Start
2006-06-01
Project End
2007-05-31
Budget Start
2006-06-01
Budget End
2007-05-31
Support Year
1
Fiscal Year
2006
Total Cost
$128,622
Indirect Cost
Name
Washington State University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
041485301
City
Pullman
State
WA
Country
United States
Zip Code
99164
Yang, Li; Tang, Xiaoting; Weisbrod, Chad R et al. (2010) A photocleavable and mass spectrometry identifiable cross-linker for protein interaction studies. Anal Chem 82:3556-66
Kaiser, Nathan K; Skulason, Gunnar E; Weisbrod, Chad R et al. (2009) A novel Fourier transform ion cyclotron resonance mass spectrometer with improved ion trapping and detection capabilities. J Am Soc Mass Spectrom 20:755-62
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
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
Shoaf-Sweeney, Kari D; Larson, Charles L; Tang, Xiaoting et al. (2008) Identification of Campylobacter jejuni proteins recognized by maternal antibodies of chickens. Appl Environ Microbiol 74:6867-75
Kaiser, Nathan K; Weisbrod, Chad R; Webb, Brian N et al. (2008) Reduction of axial kinetic energy induced perturbations on observed cyclotron frequency. J Am Soc Mass Spectrom 19:467-78
Chen, Yu-Chi; Siems, William F; Pearce, Gregory et al. (2008) Six peptide wound signals derived from a single precursor protein in Ipomoea batatas leaves activate the expression of the defense gene sporamin. J Biol Chem 283:11469-76
Anderson, Gordon A; Tolic, Nikola; Tang, Xiaoting et al. (2007) Informatics strategies for large-scale novel cross-linking analysis. J Proteome Res 6:3412-21
Chowdhury, Saiful M; Munske, Gerhard R; Ronald, Robert C et al. (2007) Evaluation of low energy CID and ECD fragmentation behavior of mono-oxidized thio-ether bonds in peptides. J Am Soc Mass Spectrom 18:493-501
Tang, Xiaoting; Yi, Wei; Munske, Gerhard R et al. (2007) Profiling the membrane proteome of Shewanella oneidensis MR-1 with new affinity labeling probes. J Proteome Res 6:724-34