Abstract
Study of structure-function relationships for biological molecules is a central theme of contemporary biomedical research. Once isolated and purified, these molecules require structural characterization before they can be used effectively to study their function in the living organism. One important subset, polypeptides, are often only available in picomole quantities. To structurally analyze these small quantities has been one goal of protein chemistry. Several methods have been developed to determine the amino acid composition, amino, acid sequence, and covalent chemical structure of polypeptides. Amino acid analysis requires only picomoles of polypeptide 1. The amino acid sequence for a polypeptide can be determined from picomole amounts by automated sequential Edman degradation followed by high performance liquid chromatographic identification of the resulting phenylthiohydantoin amino acids 2. The molecular weight and other covalent structures can be inferred from the mass spectrum of picomoles of the polypeptide. Integration of these technologies is useful in providing structural information about these small quantities.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
R.L. Henrikson and S.C. Meredith, Amino acid analysis by reverse-phase high performance liquid chromatography: precolumn derivatization with phenylisothiocyanate, Anal. Biochem. 136: 65 (1984).
M. W. Hunkapiller and L. E. Hood, New protein sequenator with increased sensitivity, Science 207: 523 (1980).
K. Biemann, Sequencing of proteins, Int. Jour, of Mass Spectrom. and Ion Physics 45: 183 (1982).
H. R. Morris, Biomolecular mass spectrometry, Int. Jour, of Mass Spectrom. and Ion Physics 45: 331 (1982).
R. D. MacFarlane, Particle-induced desorption mass spectrometry of large involatile biomolecules: surface chemistry in the high- energy short-time domain, Acc. Chem. Res. 15: 268 (1982).
B. Sundqvist, I. Kamensky, P. Hakansson, J. Kjellberg, M. Salehpour, S. Widdiyasekera, J. Fohlman, P.A. Peterson and P. Roepstorff, Californium-252 plasma desorption time of flight mass spectroscopy of proteins, Biomed. Mass Spectrom. 11: 242 (1984).
M. Barber, R. S. Bordoli, R. D. Sedgwick, A. N. Tyler, and B. N. Green, Fast atom bombardment mass spectrometry, in: Recent Developments in Mass Spectrometry in Biochemistry, Medicine, and Environmental Research, Volume 8, A. Frigerio, ed., Elsevier, Amsterdam (1983).
K. L. Busch and R. G. Cooks, Mass spectrometry of large, fragile, and involatile molecules, Science 218: 247 (1982).
A. Dell and G. W. Taylor, High-field-magnet mass spectrometry of biological molecules, Mass. Spectrom. Revs. 3: 357 (1984).
A. M. Buko, L. R. Phillips, and B. A. Fraser, Peptide studies using a fast atom bombardment high field mass spectrometer and data system. 2. Characteristics of positive ionization of peptides, m/z 858 to m/z 5729, Biomed. Mass Spectrom. 10: 408 (1983).
A. M. Buko, L. R. Phillips, and B. A. Fraser, Peptide studies using a fast atom bombardment high field mass spectrometer and data system. 1. Sample introduction, date acquisition, and mass calibration. Biomed. Mass Spectrom. 10: 324 (1983).
J. L. Gower, Matrix compounds for fast atom bombardment mass spectrometry, Biomed. Mass Spectrom. 12: 191 (1985).
G. Barany and B. Merrifield, Solid-phase peptide synthesis, in: “The Peptides, Volume 2, ” E. Gross and J. Meienhofer, eds., Academic Press, New York (1980).
A. M. Buko and B. A. Fraser, Peptide studies using a fast atom bombardment high field mass spectrometer and data system. 4. Disulfide-containing peptides, Biomed. Mass Spectrom. (in press).
S. K. Sethi, C. C. Nelson, and J. A. McCloskey, Dehalogenation reactions in fast atom bombardment mass specrometry, Analyt. Chem. 56: 1975 (1984).
A. M. Buko, L. R. Phillips, and B. A. Fraser, Peptide studies using a fast atom bombardment high field mass spectrometer and data system. 3. Negative ionization: Mass calibration, data acquisition and structural characterization. Biomed. Mass Spectrom. 10: 387 1983.
C. V. Bradley, D. H. Williams, and M. R. Hanly, Peptide sequencing using the combination of Edman degradation, carboxypeptidase digestion, and fast atom bombardment mass spectrometry, Biochem. Biophys. Res. Commun. 104: 1223 (1982).
R. Self and A. Parente, The combined use of enzymatic hydrolysis and fast atom bombardment mass spectrometry for peptide sequencing, Biomed. Mass Spectrom. 10: 78 (1983).
B. W. Gibson and K. Biemann, Strategy for the mass spectrometric verification and correction of the primary structures of proteins deduced from their DNA sequences, Proc. Natl. Acad. Sci. U.S.A. 81: 1956 (1984).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1987 Plenum Press, New York
About this chapter
Cite this chapter
Fraser, B.A. (1987). Fast Atom Bombardment Mass Spectrometry: Application to Peptide Structural Analysis. In: L’Italien, J.J. (eds) Proteins. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1787-6_26
Download citation
DOI: https://doi.org/10.1007/978-1-4613-1787-6_26
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4612-9001-8
Online ISBN: 978-1-4613-1787-6
eBook Packages: Springer Book Archive