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Protein Sequence Analysis and Domain Identification

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The Proteomics Protocols Handbook

Part of the book series: Springer Protocols Handbooks ((SPH))

Abstract

The fundamental unit of protein structure is the domain, defined as a region or regions of a polypeptide that folds independently and possesses a hydrophobic core with a hydrophilic exterior (see Note 1). Domains, particularly those with enzymatic activities, may possess functions independently of whether they are present in isolation or are part of a larger multidomain protein. Other domains confer regulatory and specificity properties to multidomain proteins, usually via the provision of binding sites. Because the majority of eukaryotic proteins, and a large number of eubacterial and archaeal proteins, are multidomain in character, the determination of the structures and functions of these proteins requires detailed consideration of their domain architectures.

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Author information

Authors and Affiliations

  1. MRC Functional Genetics Unit University of Oxford, Department of Human Anatomy and Genetics, Oxford, UK

    Chris P. Ponting

  2. European Bioinformatics Institute, Cambridge, UK

    Ewan Birney

Authors
  1. Chris P. Ponting
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  2. Ewan Birney
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Editor information

Editors and Affiliations

  1. University of Hertfordshire, Hatfield, UK

    John M. Walker

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© 2005 Humana Press Inc., Totowa, NJ

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Ponting, C.P., Birney, E. (2005). Protein Sequence Analysis and Domain Identification. In: Walker, J.M. (eds) The Proteomics Protocols Handbook. Springer Protocols Handbooks. Humana Press. https://doi.org/10.1385/1-59259-890-0:527

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  • DOI: https://doi.org/10.1385/1-59259-890-0:527

  • Publisher Name: Humana Press

  • Print ISBN: 978-1-58829-343-5

  • Online ISBN: 978-1-59259-890-8

  • eBook Packages: Springer Protocols

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