MALDI-TOF (matrix assisted laser desorption/ionization-time of flight) mass spectrometry (MS) is a state of the art method for the analysis of macromolecules such as proteins, peptides, and oligonucleotides. Recent improvements, such as delayed extraction, have had a profound impact on biological research. MALDI-TOF MS is now routinely used for high sensitivity, high performance analysis of proteins and other macromolecules, and can be used with samples from biological matrices. These uses and the features of the new generation of commercially available MALDI-TOF MS systems for dedicated use in biomedical research makes them a desirable addition to the existing shared biochemical resources within the Northwestern Drug Discovery Program. The availability of a MALDI-TOF mass spectrometer would significantly enhance the capability and productivity of NIH funded research of the major users and will allow some minor users to pursue research that was not feasible previously. The major users have prior experience with the use of MALDI-TOF MS in their funded research programs, but must use out of state resources. Currently there are no MALDI-TOF MS instruments at Northwestern University. Similarly, there is a lack of such instrumentation that is routinely available to academic-based biomedical researchers in the greater Chicago area. Therefore, funds are requested for a specific configuration of a commercially available MALDI-TOF MS instrument that is turn-key and state-of-the-art. The highly integrated and interactive user group with a documented record of sharing instrumentations and the institutional commitment make the focused use likely to succeed and the proposed instrumentation to have a high impact on multiple funded research programs.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biomedical Research Support Shared Instrumentation Grants (S10)
Project #
1S10RR013810-01
Application #
2791814
Study Section
Special Emphasis Panel (ZRG1-SSS-6 (02))
Program Officer
Tingle, Marjorie
Project Start
1999-04-15
Project End
2000-04-14
Budget Start
1999-04-15
Budget End
2000-04-14
Support Year
1
Fiscal Year
1999
Total Cost
Indirect Cost
Name
Northwestern University at Chicago
Department
Pharmacology
Type
Schools of Medicine
DUNS #
005436803
City
Chicago
State
IL
Country
United States
Zip Code
60611
Trzupek, John D; Sheppard, Terry L (2005) Photochemical generation of ribose abasic sites in RNA oligonucleotides. Org Lett 7:1493-6
Czlapinski, Jennifer L; Sheppard, Terry L (2005) Template-directed assembly and characterization of metallosalen-DNA conjugates. Bioconjug Chem 16:169-77
Chen, Lisa S; Sheppard, Terry L (2004) Chain termination and inhibition of Saccharomyces cerevisiae poly(A) polymerase by C-8-modified ATP analogs. J Biol Chem 279:40405-11
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Czlapinski, Jennifer L; Sheppard, Terry L (2004) Site-specific oxidative cleavage of DNA by metallosalen-DNA conjugates. Chem Commun (Camb) :2468-9
Wainwright, Mark S; Rossi, Janet; Schavocky, James et al. (2003) Protein kinase involved in lung injury susceptibility: evidence from enzyme isoform genetic knockout and in vivo inhibitor treatment. Proc Natl Acad Sci U S A 100:6233-8
Wang, Yingli; Sheppard, Terry L (2003) Chemoenzymatic synthesis and antibody detection of DNA glycoconjugates. Bioconjug Chem 14:1314-22
Schumacher, Andrew M; Velentza, Anastasia V; Watterson, D Martin et al. (2002) DAPK catalytic activity in the hippocampus increases during the recovery phase in an animal model of brain hypoxic-ischemic injury. Biochim Biophys Acta 1600:128-37
Mirzoeva, Salida; Sawkar, Anu; Zasadzki, Magdalena et al. (2002) Discovery of a 3-amino-6-phenyl-pyridazine derivative as a new synthetic antineuroinflammatory compound. J Med Chem 45:563-6
Velentza, A V; Schumacher, A M; Weiss, C et al. (2001) A protein kinase associated with apoptosis and tumor suppression: structure, activity, and discovery of peptide substrates. J Biol Chem 276:38956-65

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