This proposal requests support for the acquisition of an ion trap-Fourier transform ion cyclotron resonance hybrid mass spectrometer. This new instrumentation is intended for the identification and quantitation of proteins from protein complexes, whole proteomes and single cells. This instrument is arguably at the forefront of mass spectrometry instrumentation, and represents a new platform for undertaking sophisticated proteomics-related studies. Proposed use of this instrumentation will support and enhance existing NIH-funded projects and provide avenues of research support that can lead to new funding for future projects. Four NIH-supported users of this equipment will form the core research team and the value added to their research activities by this instrumentation is discussed. All of these individuals currently interact with the University of Cincinnati Mass Spectrometry (UC MS) Facility, and the identified projects are untenable or pain-staking using the equipment already in place in the UC MS Facility. Their research interests, in some form or another, cover a wide spectrum of proteomics-related investigations. Examples include the effects of environmental agents such as estrogens, metals and PAH's on proteomes; examining the underlying biochemistry associated with microorganisms as they relate to biofilm production; and understanding the lamellar body proteome. All of the investigators participating in this instrument request have vigorous and well-funded research programs. In addition, a number of other investigator's NIH-funded research would benefit from this instrument acquisition. The PI, who has been active in the field of mass spectrometry for nearly 15 years, will be responsible for the managerial oversight of the requested instrumentation. He will report to an internal advisory board composed of scientists from various UC campuses and affiliates. The internal advisory board will establish scheduling priorities, work with the PI and accounting personnel to establish cost-recovery rates, and will serve as a resource for projecting future use of the requested equipment. The equipment will be housed in the University of Cincinnati Mass Spectrometry Facility. This 3,500 sq. ft. facility was renovated in 2001 and is equipped with the ancillary instrumentation required for proteomics. The instrumentation will be operated and maintained by two Ph.D.-level facility staff scientists, with one of these scientists having prior experience in both FTMS and proteomics being designated as the primary operator. These staff scientists are supported by B.S.-level staff technicians to ensure that the services are provided in a timely manner.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biomedical Research Support Shared Instrumentation Grants (S10)
Project #
1S10RR019900-01
Application #
6803692
Study Section
Special Emphasis Panel (ZRG1-BPC-D (30))
Program Officer
Tingle, Marjorie
Project Start
2005-04-25
Project End
2006-04-24
Budget Start
2005-04-25
Budget End
2006-04-24
Support Year
1
Fiscal Year
2005
Total Cost
$918,973
Indirect Cost
Name
University of Cincinnati
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
041064767
City
Cincinnati
State
OH
Country
United States
Zip Code
45221
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Sallans, Larry; Giner, José-Luis; Kiemle, David J et al. (2013) Structural identities of four glycosylated lipids in the oral bacterium Streptococcus mutans UA159. Biochim Biophys Acta 1831:1239-49
Sallans, Larry; Giner, José-Luis; Kiemle, David J et al. (2012) Structural identities of four glycosylated lipids in the oral bacterium Streptococcus mutans UA159. Biochim Biophys Acta 1831:1239-49
Frankel, Laurie K; Sallans, Larry; Limbach, Patrick A et al. (2012) Identification of oxidized amino acid residues in the vicinity of the Mn(4)CaO(5) cluster of Photosystem II: implications for the identification of oxygen channels within the Photosystem. Biochemistry 51:6371-7
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Jones, Amy R; Bell-Horwath, Tiffany R; Li, Guorui et al. (2012) Novel oxidatively activated agents modify DNA and are enhanced by ercc1 silencing. Chem Res Toxicol 25:2542-52
Nikcevic, Irena; Wyrzykiewicz, Tadeusz K; Limbach, Patrick A (2011) DETECTING LOW-LEVEL SYNTHESIS IMPURITIES IN MODIFIED PHOSPHOROTHIOATE OLIGONUCLEOTIDES USING LIQUID CHROMATOGRAPHY - HIGH RESOLUTION MASS SPECTROMETRY. Int J Mass Spectrom 304:98-104
Castleberry, Colette M; Limbach, Patrick A (2010) Relative quantitation of transfer RNAs using liquid chromatography mass spectrometry and signature digestion products. Nucleic Acids Res 38:e162

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