Mass Spectrometric Methods for Determination of the Structure of Peptides and Proteins

  • Klaus Biemann
Part of the New Horizons in Therapeutics book series (NHTH)


Mass spectrometry (MS) has long been known as a sensitive method of characterizing compounds that are small, thermally stable, and sufficiently volatile to be vaporized into the vacuum system of the spectrometer. It was not, however, until the early 1980s that the method became applicable to large, polar molecules, with the development by Barber et al. (1981) of fast-atom-bombardment (FAB) ionization. This ionization method produces protonated molecules, (M + H)+, by bombarding a solution of the compound of interest (M)+, in a suitable liquid of very low vapor pressure, such as glycerol, with neutral atoms (or ions) of kilovolt kinetic energy.


Rabbit Bone Marrow 
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  1. Barber, M., Bordoli, R. S., Sedgwick, R. D., and Tyler, A. N., 1981, Fast atom bombardment of solids (F.A.B.): A new ion source for mass spectrometry, J. Chem. Soc., Chem. Comm. 7: 325–327.CrossRefGoogle Scholar
  2. Biemann, K., and Scoble, H. A., 1987, Characterization by tandem mass spectrometry of structural modifications in proteins, Science 237: 992–998.PubMedCrossRefGoogle Scholar
  3. Carr, S. A., and Roberts, G. D., 1986, Carbohydrate mapping by mass spectrometry: A novel method for identifying attachment sites of Asn-linked sugars in glycoproteins, Anal. Biochem. 157: 396–406.PubMedCrossRefGoogle Scholar
  4. Chatton, B., Walter, P., Ebel, J. P., Lacroute, F., and Fasiolo, F., 1988, The yeast VAS! gene encodes both mitochondria] and cytoplasmic valyl-tRNA synthetases, J. Biol. Chem. 263: 5257.Google Scholar
  5. Gibson, B. W., and Biemann, K., 1984, Strategy for the mass spectrometric verification and correction of the primary structures of proteins deduced from their DNA sequences, Proc. Natl. Acad. Sci. USA 81: 1956–1960.PubMedCrossRefGoogle Scholar
  6. Hakansson, P., Kamensky, I., Sundqvist, B., Fohlman, J., Peterson, P., McNeal, C. J., and Macfarlane, R. D., 1982, 127I-plasma desorption mass spectrometry of insulin, J. Am. Chem. Soc. 104:2948–2949.CrossRefGoogle Scholar
  7. Hill, J. A., Martin, S. A., Biller, J. E., and Biemann, K., 1988, Use of a microchannel array detector in a four-sector tandem mass spectrometer, Biomed. Environ. Mass Spectrom. 17: 147–151.PubMedCrossRefGoogle Scholar
  8. Hill, J. A., Biller, J. E., Martin, S. A., Biemann, K., Yoshidome, K., and Sato, K., 1989a, Design considerations, calibration and applications of an array detector for a four sector tandem mass spectrometer, Int. J. Mass Spectrom. Ion Processes 92: 211–230.CrossRefGoogle Scholar
  9. Hill, J. A., Biller, J. E., Martin, S. A., Biemann, K., and Ishihara, M., 1989b, A flexible array detector of extended mass range for a high performance tandem mass spectrometer, Proceedings 37th ASMS Conference on Mass Spectrometry and Allied Topics, Miami, American Society of Mass Spectrometry, pp. 1077–1078.Google Scholar
  10. Hopper, S., Johnson, R. S., Vath, J. E., and Biemann, K., 1989, Glutaredoxin from rabbit bone marrow. Purification, characterization and amino acid sequence determined by tandem mass spectrometry, J. Biol. Chem. 264: 20438–20447.PubMedGoogle Scholar
  11. Johnson, R. S., and Biemann, K., 1987, The primary structure of thioredoxin from Chromatium vinosumdetermined by high performance tandem mass spectrometry, Biochemistry 26: 1209–1214.PubMedCrossRefGoogle Scholar
  12. Johnson, R. S., and Biemann, K., 1988, Computer program for the interpretation of CID mass spectra obtained from peptides of unknown sequence, Presented at the 36th ASMS Conference on Mass Spectrometry and Allied Topics, San Francisco, CA, pp. 1398–1399.Google Scholar
  13. Johnson, R. S., Martin, S. A., Biemann, K., Stults, J. T., and Watson, J. T., 1987, Novel fragmentation process of peptides by collision induced decomposition in a tandem mass spectrometer: Differentiation of leucine and isoleucine, Anal. Chem. 59: 2621–2625.PubMedCrossRefGoogle Scholar
  14. Johnson, R. S., Mathews, W. R., Biemann, K., and Hopper, S., 1988a, Amino acid sequence of thioredoxin isolated from rabbit bone marrow determined by tandem mass spectrometry, J. Biol. Chem. 263: 9589–9597.Google Scholar
  15. Johnson, R. S., Martin, S. A., and Biemann, K., 1988b, Collision induced fragmentation of (M + H)+ ions of peptides. Side chain specific sequence ions, Int. J. Mass Spectrom. Ion Processes 86: 137–154.CrossRefGoogle Scholar
  16. Johnson, T. C., Yee, B. C., Carlson, D. E., Buchanan, B. B., Johnson, R. S., Mathews, W. R., and Biemann, K., 1988, Thioredoxin from Rhodospirillum rubrum: Primary structure and relation to thioredoxins from other photosynthetic bacteria, J. Bacteriol. 170: 2406–2408.PubMedGoogle Scholar
  17. Mueller, D. R., Eckersley, M., and Richter, W. J., 1988, Hydrogen transfer reactions in the formation of “Y + 2” sequence ions from protonated peptides, Org. Mass Spectrom. 23: 217–222.CrossRefGoogle Scholar
  18. Offner, G. D., Sawlivich, W. B., Brecher, P., Costello, C. E., and Troxler, R. F., 1988, Characterization and amino acid sequence of a fatty acid binding protein from human heart, Biochem. J. 252: 191–198.PubMedGoogle Scholar
  19. Reddy, V. A., Johnson, R. S., Biemann, K., Williams, R. S., Ziegler, F. D., Trimble, R. B., and Maley, F., 1988, Characterization of the glycosylation sites in yeast external invertase. I. N-linked oligosaccharide content of the individual sequons. J. Biol. Chem. 263: 6978–6985.PubMedGoogle Scholar
  20. Sato, K., Asada, T., Ishihara, M., Kunihiro, F., Kammei, Y., Kubota, E., Costello, C. E., Martin, S. A., Scoble, H. A., Biemann, K., 1987, High performance tandem mass spectrometry: Calibration and performance of linked scans of a four-sector instrument, Anal. Chem. 59: 1652–1659.PubMedCrossRefGoogle Scholar
  21. Scoble, H. A., Biller, J. E., and Biemann, K., 1987, A graphics display-oriented strategy for the amino acid sequencing of peptides by tandem mass spectrometry, Fresenius Z. Anal. Chem. 327: 239–245.CrossRefGoogle Scholar
  22. Shimonishi, Y., Hong, Y-M., Kitagishi, T., Matsuo, T., Matsuda, H., Katakuse, I., 1980, Sequencing of peptide mixtures by Edman degradation and field-desorption mass spectrometry, Eur. J. Biochem. 112: 251–264.PubMedCrossRefGoogle Scholar
  23. Vath, J. E., Ph.D. Thesis, Microscale derivatization of peptides and glycolipids for mass spectrometry, Massachusetts Institute of Technology, 1990.Google Scholar

Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Klaus Biemann
    • 1
  1. 1.Department of ChemistryMassachusetts Institute of TechnologyCambridgeUSA

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