Abstract

Tandem mass spectrometry (MS/MS) will be utilized to develop methods of improved specificity, sensitivity and speed to obtain structural and analytical information from larger molecules of biomedical importance. Instrumentation development will primarily involve the Fourier-transform mass spectrometer, exploiting its potentialities for high resolution MS/MS and high sensitivity for multichannel recording of full spectra, and investigating methods for efficient ion trapping. Methods studied for pulsed ionization of large molecules, especially those to produce multiply charged ions, will include SIMS with greater than or equal to 25 keV Cs+ (or larger) ions, UV laser desorption, and Cf-252 plasma desorption. Methods studied for dissociation of MS-I separated ions will include CAD at surfaces, UV photodissociation, and neutralization of one charge on a multiply charged ion. Advantages of MS/MS/MS for mixtures of peptides and other large molecules will be explored, possibly with two different ion dissociation methods. Fundamental research will continue on unimolecular ion dissociations, especially of multiply-charged and negative ions.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
2R01GM016609-19
Application #
3268967
Study Section
Metallobiochemistry Study Section (BMT)
Project Start
1977-01-01
Project End
1992-03-31
Budget Start
1987-04-01
Budget End
1988-03-31
Support Year
19
Fiscal Year
1987
Total Cost
Indirect Cost

  Institution

Name
Cornell University
Department
Type
Schools of Arts and Sciences
DUNS #
City
Ithaca
State
NY
Country
United States
Zip Code
14850

  Publications

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
Narayan, Mahesh; Welker, Ervin; Zhai, Huili et al. (2008) Detecting native folds in mixtures of proteins that contain disulfide bonds. Nat Biotechnol 26:427-9
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

Showing the most recent 10 out of 34 publications