Mass spectrometry (MS) will be utilized to develop automated methods for quantitative analysis and structure determination applicable to 10 to the minus 6th power to less than 10 to the minus 12th power g samples of biomedical importance. Methods include structure determination of complex molecules utilizing collisional activation (CA) mass spectra to determine fragment structures corresponding to individual spectral peaks, and MS/MS in which complex mixtures from biological samples are analyzed by component ionization and MS separation followed by CA identification of the separated ion species. A tandem double-focusing instrument will be applied to such studies for large biological molecules. An on-line computer system will be completed for data acquisition and feedback control for this instrument. Submicrosecond droplet vaporization will be developed as a method to obtain MS information from nonvolatile biological molecules. CA mass spectra and other techniques will be used to extend our knowledge of unimolecular ion decomposition mechanisms.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM016609-17
Application #
3268969
Study Section
Metallobiochemistry Study Section (BMT)
Project Start
1977-01-01
Project End
1986-12-31
Budget Start
1985-01-01
Budget End
1985-12-31
Support Year
17
Fiscal Year
1985
Total Cost
Indirect Cost
Name
Cornell University
Department
Type
Schools of Arts and Sciences
DUNS #
City
Ithaca
State
NY
Country
United States
Zip Code
14850
Skinner, Owen S; Breuker, Kathrin; McLafferty, Fred W (2013) Charge site mass spectra: conformation-sensitive components of the electron capture dissociation spectrum of a protein. J Am Soc Mass Spectrom 24:807-10
Begley, Tadhg P; Ealick, Steven E; McLafferty, Fred W (2012) Thiamin biosynthesis: still yielding fascinating biological chemistry. Biochem Soc Trans 40:555-60
Breuker, Kathrin; Skinner, Owen S; McLafferty, Fred W (2012) Femtosecond laser vaporization that preserves protein-folded structure: an unproven idea. Proc Natl Acad Sci U S A 109:E206; author reply E207
Skinner, Owen S; McLafferty, Fred W; Breuker, Kathrin (2012) How ubiquitin unfolds after transfer into the gas phase. J Am Soc Mass Spectrom 23:1011-4
Kong, Xianglei; Lin, Cheng; Infusini, Giuseppe et al. (2009) Numerous isomers of serine octamer ions characterized by infrared photodissociation spectroscopy. Chemphyschem 10:2603-6
Han, Xuemei; Smith, Norah L; Sil, Dwaipayan et al. (2009) IgE receptor-mediated alteration of membrane-cytoskeleton interactions revealed by mass spectrometric analysis of detergent-resistant membranes. Biochemistry 48:6540-50
Steinberg, Michal Z; Elber, Ron; McLafferty, Fred W et al. (2008) Early structural evolution of native cytochrome c after solvent removal. Chembiochem 9:2417-23
Breuker, Kathrin; Jin, Mi; Han, Xuemei et al. (2008) Top-down identification and characterization of biomolecules by mass spectrometry. J Am Soc Mass Spectrom 19:1045-53
Breuker, Kathrin; McLafferty, Fred W (2008) Stepwise evolution of protein native structure with electrospray into the gas phase, 10(-12) to 10(2) s. Proc Natl Acad Sci U S A 105:18145-52
McLafferty, Fred W (2008) Mass spectrometry across the sciences. Proc Natl Acad Sci U S A 105:18088-9

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