This revised application describes an efficient and economical plan for our newly reorganized Mass Spectrometry Facility to serve the five missions of BRTP. A central staff will provide technical support for operation and maintenance of instruments, training, interpretation of data, and supervision of research associates involved in Technological Research and Development (TRD) projects involving the development of chemical and instrumental approaches to structure analysis of MALDL ions in the analysis of biopolymers. The research associates also will serve as interactive liaisons between our user community and independently- funded research projects of the Facility's co-investigators and PIs. This proposed active interaction with several associated independently funded projects will enrich the technology base available to users and help ensure that efforts in TRD are directed toward the needed of users of the Facility. Interaction with the Macromolecular Structure (Peptide) Facility, located adjacent to the Mass Spectrometry Facility, will continue to enhance the expertise and capabilities of each facility in serving its users. The Mass Spectrometry Facility houses nine mass spectrometers, five of which are dedicated principally to the interests of more than 80 biomedical investigators in the local, regional, and national scientific community. The Mass Spectrometry Facility is a shared University Facility in that MSU has assisted in the acquisition of major equipment to stimulate innovative research activities and to provide a state-of- the-art instrumentation and research base on campus. Training continues to be a major activity of the Mass Spectrometry Facility where approximately 20 Ph.D. graduate students are conducting research under the direction of the PIs and co-investigators. However, no financial support is requested in this application for graduate students. Support is requested for three research associates who will obtain advanced training in mass spectrometry and who, along with the PIs and co- investigators, will conduct TRD in the Mass Spectrometry Facility. Formal training in mass spectrometry is available through academic programs at MSU as well as via an outreach program in the form of a Short Course sponsored by the American Chemical Society both as an off-campus lecture-only version and as a five-day on-campus """"""""hands-on"""""""" program.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR000480-26
Application #
2281279
Study Section
Special Emphasis Panel (ZRG7-SSS-6 (10))
Project Start
1978-01-01
Project End
1998-05-31
Budget Start
1995-06-01
Budget End
1996-05-31
Support Year
26
Fiscal Year
1995
Total Cost
Indirect Cost
Name
Michigan State University
Department
Biochemistry
Type
Schools of Medicine
DUNS #
193247145
City
East Lansing
State
MI
Country
United States
Zip Code
48824
Peri, S P; Bhadti, V S; Somerville-Armstrong, K S et al. (1999) Affinity reagents for cross-linking hemoglobin: bis(phenoxycarbonylethyl)phosphinic acid (BPCEP) and bis(3-nitrophenoxycarbonylethyl)phosphinic acid (BNCEP). Hemoglobin 23:1-20
Chen, H M; Sood, R; Hosmane, R S (1999) An efficient, short synthesis and potent anti-hepatitis B viral activity of a novel ring-expanded purine nucleoside analogue containing a 5:7-fused, planar, aromatic, imidazo[4,5-e][1,3]diazepine ring system. Nucleosides Nucleotides 18:331-5
Bretner, M; Beckett, T D; Sood, R K et al. (1999) Substrate/inhibition studies of bacteriophage T7 RNA polymerase with the 5'-triphosphate derivative of a ring-expanded ('fat') nucleoside possessing potent antiviral and anticancer activities. Bioorg Med Chem 7:2931-6
Agasimundin, Y S; Mumper, M W; Hosmane, R S (1998) Inhibitors of glycogen phosphorylase b: synthesis, biochemical screening, and molecular modeling studies of novel analogues of hydantocidin. Bioorg Med Chem 6:911-23
Hosmane, R S; Peri, S P; Bhadti, V S et al. (1998) Bis[2-(4-carboxyphenoxy)carbonylethyl]phosphinic acid (BCCEP): a novel affinity reagent for the beta-cleft modification of human hemoglobin. Bioorg Med Chem 6:767-83
Rajappan, V P; Hosmane, R S (1998) Analogues of azepinomycin as inhibitors of guanase. Nucleosides Nucleotides 17:1141-51
Hosmane, R S; Hong, M (1997) How important is the N-3 sugar moiety in the tight-binding interaction of coformycin with adenosine deaminase? Biochem Biophys Res Commun 236:88-93
Lopez-Lara, I M; Orgambide, G; Dazzo, F B et al. (1993) Characterization and symbiotic importance of acidic extracellular polysaccharides of Rhizobium sp. strain GRH2 isolated from acacia nodules. J Bacteriol 175:2826-32
Watson, J T; Kayganich, K (1989) Novel sample preparation for analysis by electron capture negative ionization mass spectrometry. Biochem Soc Trans 17:254-7
Kassel, D B; Kayganich, K A; Watson, J T et al. (1988) Utility of ion source pretreatment with chlorine-containing compounds for enhanced performance in gas chromatography/negative ionization mass spectrometry. Anal Chem 60:911-7

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