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Proteases in Peptide Mapping and Sequencing

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Proteolytic Enzymes

Part of the book series: Springer Lab Manual ((SLM))

Abstract

The ability of some proteases to cleave polypeptide chains at restricted cleavage sites makes them important tools for the elucidation of the primary and even higher-order structure of proteins. This chapter provides an introduction into the methodology of enzymatic protein fragmentation. In addition, a series of complementary chemical methods are included which are indispensable for protein sequence analysis and peptide mapping. The specificity of most endopeptidases show a strong preference for particular amino acid residues or short sequence recognition sites. The chemical neighborhood of these residues, i.e. the character of their side chains, like hydrophobicity or size, may influence the rate of hydrolysis.

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Authors and Affiliations

  1. Max-Planck-Institüt für Biochemie, Arbeitsgruppe Proteinanalytik, Am Klopferspitz 18a, Martinsried, 82152, Germany

    Josef Kellermann

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  1. Josef Kellermann
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Editors and Affiliations

  1. Institut für Biochemie und Molekularbiologie, Universität Bern, Bühlstrasse 28, CH-3012, Bern, Germany

    Erwin E. Sterchi

  2. Institut für Zoophysiologie, Westfälische Wilhelms-Universität Münster, Hindenburgplatz 55, D-48143, Münster, Germany

    Walter Stöcker

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© 1999 Springer-Verlag Berlin Heidelberg

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Kellermann, J. (1999). Proteases in Peptide Mapping and Sequencing. In: Sterchi, E.E., Stöcker, W. (eds) Proteolytic Enzymes. Springer Lab Manual. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-59816-6_14

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  • DOI: https://doi.org/10.1007/978-3-642-59816-6_14

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-47807-9

  • Online ISBN: 978-3-642-59816-6

  • eBook Packages: Springer Book Archive

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