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Analysis of Hydrophobic Proteins and Peptides by Mass Spectrometry

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Mass Spectrometry of Proteins and Peptides

Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 146))

Abstract

The introduction of electrospray ionization mass spectrometry (ESI-MS) (1) and matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) (2) in the late eighties has had a tremendous influence on the analysis of biomolecules at the molecular level in biochemistry and biology. The vast number of publications dealing with many different aspects of biomolecules has, however, focused primarily on water-soluble compounds (3). The poor solubility and scarcity of hydrophobic peptides and proteins has hampered extensive analysis of these materials by ESI-MS or by MALDI-MS.

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Authors and Affiliations

  1. Department für Chemie und Biochemie, Universität Bern,Freiestrasse, Bern, Switzerland

    Johann Schaller

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  1. Johann Schaller
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Editors and Affiliations

  1. Sale, Manchester, UK

    John R. Chapman

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© 2000 Humana Press Inc.

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Schaller, J. (2000). Analysis of Hydrophobic Proteins and Peptides by Mass Spectrometry. In: Chapman, J.R. (eds) Mass Spectrometry of Proteins and Peptides. Methods in Molecular Biology™, vol 146. Humana Press, Totowa, NJ. https://doi.org/10.1385/1-59259-045-4:425

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  • DOI: https://doi.org/10.1385/1-59259-045-4:425

  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-0-89603-609-3

  • Online ISBN: 978-1-59259-045-2

  • eBook Packages: Springer Protocols

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