Skip to main content
SpringerLink
Log in

Mass Spectrometry in Protein Structural Analysis

  • Chapter
Physical Methods to Characterize Pharmaceutical Proteins

Part of the book series: Pharmaceutical Biotechnology ((PBIO,volume 7))

  • 235 Accesses

Abstract

Mass spectrometric protein analysis was pioneered in the 1960s and early 1970s by K. Biemann and co-workers at MIT, E. Lederer’s group at the Institute for Natural Product Chemistry in Gif sur Yvette, France, in collaboration with M. Barber at AEI, and at the Shemyakin Institute for Natural Product Chemistry in Moscow. The mass spectrometric techniques at that time required volatile samples that, because of the zwitter ionic nature of peptides, required derivatization. Ionization was performed by electron impact, resulting in high excitation of the formed ions and subsequent extensive fragmentation. As a result, only rather small peptides were amenable to mass spectrometric analysis. The development of new ionization methods in the 1970s such as chemical ionization and field desorption, although promising, did not improve the perspectives for mass spectrometric protein analysis. In spite of these limitations, mass spectrometric research, carried out in a rather limited number of groups, made significant contributions to protein research, especially in characterization of posttranslationally modified amino acid residues and sequencing of N-terminally blocked peptides (reviewed, for exam-ple, in Arpino and McLafferty, 1976).

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 129.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 169.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 169.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Andersen, J. S., Andersen, S. O., Højrup, P., and Roepstorff, P., 1993, Primary structure of a 14 kDa protein (Lm-76) from the cuticle of the migratory locust, Locusta migratoria, Insect Biochem. Molec. Biol. 23:391–402.

    Article  CAS  Google Scholar 

  • Andersen, S. O., Rafn, K., Krogh, T. N., Højrup, P., and Roepstorff, P., 1995, Comparison of larval and pupal cuticular protein in Tenebrio molitor, Insect Biochem. Mol Biol. 25: 177–188.

    Article  PubMed  CAS  Google Scholar 

  • Andreasen, L., Højrup, P., Andersen, S. O., and Roepstorff, P., 1992, Combined plasma desorption mass spectrometry and Edman degradation applied to simultaneous sequence determination of isoforms of structural proteins from cuticle of Locusta migratoria, Eur. J. Biochem. 217:267–273.

    Article  Google Scholar 

  • Arpino, P. J., and McLafferty, F. W., 1976, Amino acid sequencing of oligopeptides by mass spectrometry, in: Determination of Organic Structures by Physical Methods, Vol. 6 (F. C. Nachod, J. J. Zuckerman, and E. W. Randall, eds.), Academic Press, New York, pp. 1–80.

    Chapter  Google Scholar 

  • Balloul, J. M., Grzych, J. M., Pierce, R. J., and Capron, A., 1987, A purified 28 kDa protein from Schistosoma mansoni adult worms protect rats and mice against experimental schistosomaisis, J. Immunol 138:3448–3453.

    PubMed  CAS  Google Scholar 

  • 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. Commun. 1981:325–327.

    Article  Google Scholar 

  • Barber, M., Bordoli, R. S., Elliot, G. J., Sedgwick, R. D., Tyler, A. N., and Green, B. N., 1982, Fast atom bombardment mass spectrometry of bovine insulin and other large peptides, J. Chem. Soc. Chem. Commun. 1982:936–938.

    Article  Google Scholar 

  • Beavis, R. C., 1992a, Matrix-assisted ultraviolet laser desorption: Evolution and principles, Org. Mass Spectrom. 27:653–659.

    Article  CAS  Google Scholar 

  • Beavis, R. C., 1992b, Phenomenological models for matrix-assisted laser desorption ion yields near the threshold fluence, Org. Mass Spectrom. 27:864–868.

    Article  CAS  Google Scholar 

  • Beavis, R. C., and Chait, B. T., 1990, Rapid sensitive analysis of protein mixtures by mass spectrometry, Proc. Natl. Acad. Sci. USA 87:6873–6877.

    Article  PubMed  CAS  Google Scholar 

  • Biemann, K., 1988, Contributions of mass spectrometry to peptide and protein structure, Biomed. Environ. Mass Spectrom. 16:99–111.

    Article  PubMed  CAS  Google Scholar 

  • Biemann, K., 1990, Sequencing of peptides by tandem mass spectrometry and high-energy collision-induced dissociation, in: Methods in Enzymology, Vol. 193 (J. A. McCloskey, ed.), Academic Press, San Diego, CA, pp. 455–479.

    Google Scholar 

  • Boucheron, B., Jacquinod, M., Klarskov, K., Trottein, F., Klein, M., Van Doersselaer, A., Bischoff, R., and Roitsch, C., 1994, Analysis of the primary structure and post-translational modifications of the Schistosoma mansoni antigen Smp28, J. Chromatogr. B662:279–290.

    Google Scholar 

  • Caprioli, R., and Suter, M. J. F., 1992, Continuous flow fast atom bombardment: Recent advances and applications, Int. J. Mass Spectrom. Ion Proc. 118/119:449–476.

    Article  Google Scholar 

  • Carr, S. A., Hemling, M. E., Folena-Wasserman, G., Sweet, R. W., Anumula, K., Barr, J. R., Huddleston, M. J., and Taylor, P. J., 1989, Protein and carbohydrate structural analysis of a recombinant soluble CD4 receptor by mass spectrometry, J. Biol. Chem. 264:21286–21295.

    PubMed  CAS  Google Scholar 

  • Cherfas, F., 1991, New hope for vaccine against schistosomiasis, Science 251:630–631.

    Article  PubMed  CAS  Google Scholar 

  • Chowdhury, S. K., Katta, V., and Chait, B. T., 1990, An electrospray-ionization with new features, Rapid Commun. Mass Spectrom. 4:81–87.

    Article  PubMed  CAS  Google Scholar 

  • Dell, A., and Morris, H. R., 1982, Fast atom bombardment-high field magnetic mass spectrometry of 6000 dalton polypeptides, Biochem. Biophys. Res. Commun. 106: 1456–1461.

    Article  PubMed  CAS  Google Scholar 

  • Desiderio, D. M., 1991, Mass Spectrometry of Peptides, CRC Press, Boca Raton, FL.

    Google Scholar 

  • Dole, M., Mack, L. L., Hines, R. L., Mobley, R. C., Ferguson, L. O., and Alice, M. B., 1968, Molecular beams of macroions, J. Chem. Phys. 49:2240–2249.

    Article  CAS  Google Scholar 

  • Egorov, T. A., Musolyamov, A. Kh., Andersen, J. S., and Roepstorff, P., 1994, The complete amino acid sequence and disulphide bond arrangement of oat alcohol-soluble avenin-3, Eur. J. Biochem. 224:631–638.

    Article  PubMed  CAS  Google Scholar 

  • Fenn, J. B., Mann, M., Meng, C. K., Wong, S. F., and Whitehouse, C. M., 1989, Electrospray ionization for mass spectrometry of large biomolecules, Science 246:64–71.

    Article  PubMed  CAS  Google Scholar 

  • Goldberg, D. E., Slater, A. F. G., Beavis, R., Chait, B., Cerami, A., Henderson, G. B., 1991, Hemoglobin degradation in the human malaria pathogen Plasmodium falciparum: A catabolic pathway initiated by a specific aspartic protease, J. Exp. Med. 173:961–969.

    Article  PubMed  CAS  Google Scholar 

  • Green, B. N., Oliver, R. W. A., Falick, A. M., Schackelton, C. M. L., Roitman, E., and Witkanska, H. L., 1990, Electrospray MS, LSIMS and MS/MS for the rapid detection and characterization of variant hemoglonins, in: Biological Mass Spectrometry (A. L. Burlingame and J. A. McCloskey, eds.), Elsevier, Amsterdam, pp. 129–146.

    Google Scholar 

  • Haebel, S., Jensen, C., Andersen, S. O., and Roepstorff, P., 1995, Isoforms of a cuticular protein from larvae of the meal beetle, Tenebrio moletor, studied by mass spectrometry in combination with Edman degradation and 2D-PAGE, Protein Science, 4:394–404.

    Article  PubMed  CAS  Google Scholar 

  • HÃ¥kansson, P., Kamensky, I., Sundqvist, B., Fohlman, J., Peterson, P., McNeal, C. J., and Macfarlane, R. D., 1982, 127-I Plasma desorption mass spectrometry of insulin, J. Am. Chem. Soc. 104:2948–2949.

    Article  Google Scholar 

  • Henzel, W. J., Billed, T. M., Stults, J. T., Wong, S. C., Grimley, C., and Watanabe, C., 1993, Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases, Proc. Natl. Acad. Sci. USA 90:5011–5015.

    Article  PubMed  CAS  Google Scholar 

  • Hillenkamp, F., 1989, Laser desorption mass spectrometry: Mechanisms, techniques and applications, in: Advances in Mass Spectrometry, Vol. 11A (P. Longevialle, ed.), Heyden and Sons, London, pp. 354–362.

    Google Scholar 

  • Hillenkamp, F., Karas, M., Ingendoh, A., and Stahl, B., 1990, Matrix assisted UV-laser desorption/ionization: A new approach to mass spectrometry of large biomolecules, in: Biological Mass Spectrometry (A. L. Burlingame and J. A. McCloskey, eds.), Elsevier, Amsterdam, pp. 49–58.

    Google Scholar 

  • Højrup, P., Andersen, S. O., Roepstorff, P., 1986, Primary structure of a structural protein from the cuticle of the migratory locust, Locusta migratoria, Biochem. J. 236: 713–720.

    Google Scholar 

  • Højrup, P., Gerola, P., Mikkelsen, J., Hansen, H. F., El-Shahed, A., Knudsen, J., Roepstorff, P., and Olson, J. M., 1991, The primary structure of the bacteriochlorophyl c-binding protein from chlorosomes of Chlorobium limicola f. thiosulfatophilum, Biochem. Biophys. Acta 1077:220–224

    Article  PubMed  Google Scholar 

  • Hopper, S., Johnson, R. S., Vath, J. E., and Biemann, K., 1989, Glutaredoxin from rabbit bone marrow, J. Biol. Chem. 264:20438–20447.

    PubMed  CAS  Google Scholar 

  • Hunt, D. F., Yates III, J. R., Shabanowitz, J., Bruns, M. E., and Bruns, D. E., 1989, Amino acid sequence analysis of two mouse calbindin-D9k isoforms by tandem mass spectrometry, J. Biol. Chem. 264:6580–6586.

    PubMed  CAS  Google Scholar 

  • Hunt, D. E, Shabanowitz, J., Griffin, P. R., Yates III, J. R., Martino, P. A., and McCormack, A. L., 1990, Protein and oligopeptide sequence analysis by triple quadrupole and quadrupole fourier transform mass spectrometry, in: Biological Mass Spectrometry (A. L. Burlingame and J. A. McCloskey, eds.), Elsevier, Amsterdam, pp. 337–362.

    Google Scholar 

  • James, P., Quadroni, M., Carafoli, E., and Gonnet, G., 1993, Protein identification by mass profile fingerpringing, Biochem. Biophys. Res. Commun. 195:58–64.

    Article  PubMed  CAS  Google Scholar 

  • Jensen, O. N., Højrup, P., and Roepstorff, P., 1991, Plasma desorption mass spectrometry as a tool in characterization of abnormal proteins. Application to variant human hemoglobins, Anal. Biochem. 199:175–183.

    Article  PubMed  CAS  Google Scholar 

  • Jespersen, S., Højrup, P., Andersen, S.O., and Roepstorff, P., 1994, The primary structure of an endocuticular protein from two locust species, Locusta migratoria and Schistocerca gregaria, determined by a combination of mass spectrometry and automatic Edman degradation, Comp. Biochem. Physiol. 109B:125–138.

    CAS  Google Scholar 

  • Jonsson, G. P., Hedin, A. B., HÃ…kansson, P. L., Sundqvist, B. U. R., Säve, G. S., Nielsen, P. F., Roepstorff, P., Johansson, K. E., Kamensky, I., and Lindberg, M. S. L., 1986, Plasma desorption mass spectrometry of peptides and proteins absorbed on nitrocellulose, Anal. Chem. 58:1084–1087.

    Article  CAS  Google Scholar 

  • Karas, M., and Hillenkamp, F., 1988, Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons, Anal. Chem. 60:2299–2301.

    Article  PubMed  CAS  Google Scholar 

  • Karas, M., Ingendoh, A., Bahr, U., and Hillenkamp, F., 1989a, Ultraviolet-laser desorption/ ionization mass spectrometry of femtomolar amounts of large proteins, Biomed. Environ. Mass Spectrom. 18:841–843.

    Article  CAS  Google Scholar 

  • Karas, M., Bahr, U., Ingendoh, A., and Hillenkamp, F., 1989b, Laser desorption mass spectrometry of mass 100,000 to 250,000, Angew. Chem. Int. 28:760–761.

    Article  Google Scholar 

  • Karas, M., Bahr, U., Ingendoh, A., Nordhoff, E., Stahl, B., Strupat, K., Hillenkamp, F., 1990, Principles and applications of matrix-assisted UV-laser desorption/ionization mass spectrometry, Anal. Chim. Acta 1990:175–185.

    Article  Google Scholar 

  • Katta, V., and Chait, B. T., 1991a, Conformational changes in proteins probed by hydrogenexchange electrospray-ionization mass spectrometry, Rapid Commun. Mass Spectrom. 5:214–217.

    Article  PubMed  CAS  Google Scholar 

  • Katta, V., and Chait, B. T., 1991b, Observation of the heme-globin complex in native myoglobin by electrospray-ionization mass spectrometry, J. Am. Chem. Soc. 113: 8534–8535.

    Article  CAS  Google Scholar 

  • Katta, V., Chowdhury, S. K., and Chait, B. T., 1991, Use of a single-quadrupole mass spectrometer for collision-induced dissociation studies of multiply charged peptide ions produced by electrospray ionization, Anal. Chem. 63:174–178.

    Article  PubMed  CAS  Google Scholar 

  • Kaur, S., Medzihradszky, K. F., Yu, Z., Baldwin, M. A., Gillece-Castro, B. L., Walls, F. C., Gibson, B. W., and Burlingame, A. L., 1990, in: Biological Mass Spectrometry (A. L. Burlingame and J. A. McCloskey, eds.), Elsevier, Amsterdam, pp. 285–309.

    Google Scholar 

  • Klarskov, K., Højrup, P., Andersen, S.O., and Roepstorff, P., 1989, Plasma desorption mass spectrometry as an aid in protein sequence determination. Application of the method on a cuticular protein from the migratory locust, Biochem. J. 262:923–930.

    PubMed  CAS  Google Scholar 

  • Klarskov, K., Roecklin, D., Bouchon, B., Sabatié, J., Van Doersselaer, A., and Bischoff, R., 1994, Analysis of recombinant Schistosoma mansoni antigen rSmp28 by on-line liquid chromatography mass spectrometry combined with sodium dodecylsulfate polyacrylamide electrophoresis, Anal. Biochem. 216:127–134.

    Article  PubMed  CAS  Google Scholar 

  • Knight, W. B., Swiderek, K. M., Sakuma, T., Calaycay, J., Shiveley, J. E., Lee, T. D., Cover, T. R., Shushan, B., Green, B. G., Cabin, R., Shah, S., Mumford, R., Dickinson, T. A., and Griffin, P. R., 1993, Electrospray ionization mass spectrometry as a mechanistic tool: Mass of human leucocyte elastase and a β-lactam-derived E-I complex, Biochemistry 32:2031–2035.

    Article  PubMed  CAS  Google Scholar 

  • Knudsen, J., Højrup, P., Hansen, H. O., Hansen, F. H., and Roepstorff, P., 1989, Acyl-CoA-binding protein in rat: Purification, binding characteristics, tissue concentrations and amino acid sequence, Biochem. J. 262:513–519.

    PubMed  CAS  Google Scholar 

  • Krogh, T. N., Skou, L., Roepstorff, P., Andersen, S. O., and Højrup, P., 1995, Primary structure of protein from the wing cuticle of the migratory locust, Locusta migratoria, Insect Biochem. Mol. Biol., 25:319–329.

    Article  CAS  Google Scholar 

  • Loo, J. A., Loo, R. R. O., Udseth, H. R., Edmonds, C. G., and Smith, R. D., 1991, Solvent-induced conformational changes of polypeptides probed by electrospray-ionization mass spectrometry, Rapid Commun. Mass Spectrom. 5:101–105.

    Article  PubMed  CAS  Google Scholar 

  • Mann, M., 1990, Electrospray: Its potential and limitations as an ionization method for biomolecules, Org. Mass Spectrom. 25:575–587.

    Article  CAS  Google Scholar 

  • Mann, M., Højrup, P., and Roepstorff, P., 1992, Use of mass spectrometric molecular weight information to identify proteins in sequence databases, Biol. Mass Spectrom. 22: 338–345.

    Article  Google Scholar 

  • McLafferty, F. W., 1992, Presented at the meeting on Biological Mass Spectrometry, Kyoto, September 1992.

    Google Scholar 

  • Mikkelsen, J., Højrup, P., Nielsen, P. F., Roepstorff, P., and Knudsen, J., 1987, Amino acid sequence of Acyl-CoA-binding protein from cow liver, Biochem. J. 245:857–861.

    PubMed  CAS  Google Scholar 

  • Mørtz, E., Vorm, O., Mann, M., and Roepstorff, P., 1994, Identification of proteins in polyacrylamide gels by mass spectrometric peptide mapping combined with database search, Biol. Mass Spectrom. 23:249–261.

    Article  PubMed  Google Scholar 

  • Naylor, S., Findeis, A. F., Gibson, B. W., and Williams, D. H., 1986, An approach towards the complete FAB analysis of enzymic digests of peptides and proteins, J. Am. Chem. Soc. 108:6359–6363.

    Article  CAS  Google Scholar 

  • Nielsen, P. F., and Roepstorff, P., 1989, Suppression effects in peptide mapping by plasma desorption mass spectrometry, Biomed. Environm. Mass Spectrom. 18:131–137.

    Article  CAS  Google Scholar 

  • Pappin, D. J. C., Højrup, P., and Bleasby, A. J., 1993, Rapid identification of proteins by peptide-mass fingerprinting, Curr. Biol. 3:327–332.

    Article  PubMed  CAS  Google Scholar 

  • Rasmussen, H., Mørtz, E., Mann, M., Roepstorff, P., and Celis, J. E., 1994, Identification of transformation sensitive proteins recorded in human two dimensional gel protein databases by mass spectrometric peptide mapping alone and in combination with microsequencing, Electrophoresis 15:406–416.

    Article  PubMed  CAS  Google Scholar 

  • Roepstorff, P., 1990, Sample preparation for plasma desorption mass spectrometry, in: Methods in Enzymology, Vol. 193 (J. A. McCloskey, ed.), Academic Press, San Diego, CA, pp. 432–440.

    Google Scholar 

  • Roepstorff, P., and Fohlman, J., 1984, Proposal for a common nomenclature for sequence ions in mass spectra of peptides, Biomed. Mass Spectrom. 11:601.

    Article  PubMed  CAS  Google Scholar 

  • Roepstorff, P., and Højrup, P., 1992, A general strategy for the use of molecular weight information in protein purification and sequence determination, in: Methods in Protein Sequence Analysis 1992 (K. Imahori and F. Sakiyama, eds.), Plenum Press, New York, pp. 149–156.

    Google Scholar 

  • Roepstorff, P., Klarskov, K., and Højrup, P., 1989, Strategy for the use of plasma desorption mass spectrometry in protein sequence analysis, in: Methods in Protein Sequence Analysis 1988 (B. Wittmann-Liebold, ed.), Springer Verlag, Berlin, pp. 191–198.

    Chapter  Google Scholar 

  • Roepstorff, P., Talbo, G., Klarskov, K., and Højrup, P., 1990, Nitrocellulose, the interface between plasma desorption mass spectrometry and protein chemistry, in: Biological Mass Spectrometry (A. L. Burlingame and J. A. McCloskey, eds.), Elsevier, Amsterdam, pp. 25–48.

    Google Scholar 

  • Roepstorff, P., Klarskov, K., Andersen, J., Mann, M., Vorm, O., Etienne, G., and Parello, J., 1991, Mass spectrometry of proteins: Studies of parvalbumins by plasma desorption, laser desorption and electrospray mass spectrometry, Int. J. Mass Spectrom. Ion Proc. 111:151–172.

    Article  CAS  Google Scholar 

  • Roepstorff, P., Schram, K. H., Andersen, J. S,. Rafn, K., Baldursson, T., Krøll, J., Poulsen, K., Knudsen, J., and Kristiansen, K., 1995, Evaluation of mass spectrometric techniques for characterization of engineered proteins, Molecular Biotechnology, in press.

    Google Scholar 

  • Scrieller, H. V., Okkels, J. S., Høj, P. B., Svendsen, I., Roepstorff, P., and Møller, B. L., 1989, The primary structure of a 4.0-kDa photosystem I polypeptide encoded by the chloroplast psal gene, J. Biol. Chem. 264:18402–18406.

    Google Scholar 

  • Scrieller, H. V., Okkels, J. S., Roepstorff, P., Jepsen, L. B, and Møller, B. L., 1990, Characterization of a cDNA clone for the PsaE gene from barley and plasma desorption mass spectrometry of the corresponding photosystem I polypeptide PSI-E, in: Proceedings of the VIIIth International Congress on Photosynthesis, Stockholm, August (M. Baltscheffsky, ed.), Klüwer Academic Publishers, Dortrecht, pp. 609–612.

    Google Scholar 

  • Smith, R. D., and Light-Wahl, K. J., 1993, The observation of non-covalent interactions in solution by electrospray ionization mass spectrometry: Promise, pitfalls and prognosis, Biol. Mass Spectrom. 22:493–501.

    Article  CAS  Google Scholar 

  • Smith, R. D., Loo, J. A., Edmonds, C. G., Barinaga, C. J., and Udseth, H. R., 1990, New developments in biochemical mass spectrometry: Electrospray ionization, Anal. Chem. 62:882–899.

    Article  PubMed  CAS  Google Scholar 

  • Sorensen, H. H., Thomsen, J., Bayne, S., Højrup, P., and Roepstorff, P., 1990, Strategies for determination of disulfide bridges in proteins using plasma desorption mass spectrometry, Biomed. Environ. Mass Spectrom. 19:713–720.

    Article  PubMed  CAS  Google Scholar 

  • Stults, J. T, Bourell, J. H., Canova-Davis, E., Ling, V. T., Laramee, G. R., Winslow, J. W., Griffin, P. R., Rinderknecht, E., and Vandlen, R. L., 1990, Structural characterization by mass spectrometry of native and recombinant human relaxin, Biomed. Environ. Mass Spectrom. 19:655–664.

    Article  PubMed  CAS  Google Scholar 

  • Sundqvist, B., Roepstorff, P., Fohlman, J., Hedin, A., HÃ¥kansson, P., Kamensky, I., Lindberg, M., Sahlepour, M., and Säve, G., 1984, Molecular weight determination of proteins by Californium plasma desorption mass spectrometry, Science 226:696–698.

    Article  PubMed  CAS  Google Scholar 

  • Talbo, G., Højrup, P., Rahbek-Nielsen, H., Andersen, S. O., and Roepstorff, P., 1990, Determination of the covalent structure of an N-and C-terminally blocked glycoprotein from endocuticle of Locusta migratoria. Combined use of plasma desorption mass spectrometry and Edman degradation to study post-translationally modified proteins, Eur. J. Biochem. 195:495–504.

    Article  Google Scholar 

  • Torgerson, D. F., Skowronski, R. P., and Macfarlane, R. D., 1974, New approach to the mass spectrometry of non-volatile compounds, Biochem. Biophys. Res. Commun. 60: 616–621.

    Article  PubMed  CAS  Google Scholar 

  • Vestling, M. M., Murphy, C. M., and Fenselau, C., 1990, Recognition of trypsin autolysis products by high-performance liquid chromatography and mass spectrometry, Anal. Chem. 62:2391–2394.

    Article  PubMed  CAS  Google Scholar 

  • Wang, R., Chen, L., and Cotter, R. J., 1990, Effects of peptide hydrophobicity and charge state on molecular ion yields in plasma desorption mass spectrometry, Anal Chem. 62: 1700–1705.

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Molecular Biology, Odense University, DK-5230, Odense M., Denmark

    Peter Roepstorff

Authors
  1. Peter Roepstorff
    View author publications

    You can also search for this author in PubMed Google Scholar

Editor information

Editors and Affiliations

  1. University of Utah, Salt Lake City, Utah, USA

    James N. Herron

  2. National Institute of Public Health and Environmental Protection, Bilthoven, The Netherlands

    Wim Jiskoot

  3. Groningen-Utrecht Institute for Drug Exploration, Utrecht University, and Utrecht Institute for Pharmaceutical Sciences, Utrecht, The Netherlands

    Daan J. A. Crommelin

Rights and permissions

Reprints and permissions

Copyright information

© 1995 Springer Science+Business Media New York

About this chapter

Cite this chapter

Roepstorff, P. (1995). Mass Spectrometry in Protein Structural Analysis. In: Herron, J.N., Jiskoot, W., Crommelin, D.J.A. (eds) Physical Methods to Characterize Pharmaceutical Proteins. Pharmaceutical Biotechnology, vol 7. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1079-0_4

Download citation

  • DOI: https://doi.org/10.1007/978-1-4899-1079-0_4

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4899-1081-3

  • Online ISBN: 978-1-4899-1079-0

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation