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Conformational Disorder

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Data Mining Techniques for the Life Sciences

Part of the book series: Methods in Molecular Biology ((MIMB,volume 609))

Abstract

In recent years it was shown that a large number of proteins are either fully or partially disordered. Intrinsically disordered proteins are ubiquitary proteins that fulfill essential biological functions while lacking a stable 3D structure. Despite the large abundance of disorder, disordered regions are still poorly detected. The identification of disordered regions facilitates the functional annotation of proteins and is instrumental in delineating boundaries of protein domains amenable to crystallization. This chapter focuses on the methods currently employed for predicting disorder and identifying regions involved in induced folding.

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Acknowledgments

MeDor was developed with the financial support of the EU VIZIER (http://www.vizier-europe.org). program (CT 2004-511960) and the ANR (ANR-05-MIIM-035-02).

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Authors and Affiliations

  1. Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS et Universités Aix-Marseille I et II, Marseille, France

    Sonia Longhi, Philippe Lieutaud & Bruno Canard

Authors
  1. Sonia Longhi
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  2. Philippe Lieutaud
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  3. Bruno Canard
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Editor information

Editors and Affiliations

  1. Max F. Perutz Laboratories GmbH, Universität Wien, Dr. Bohr-Gasse 9, Wien, 1030, Austria

    Oliviero Carugo

  2. Research (A*STAR), Agency for Science & Technology, Biopolis Street 30, Singapore, 138671, Singapore

    Frank Eisenhaber

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Longhi, S., Lieutaud, P., Canard, B. (2010). Conformational Disorder. In: Carugo, O., Eisenhaber, F. (eds) Data Mining Techniques for the Life Sciences. Methods in Molecular Biology, vol 609. Humana Press. https://doi.org/10.1007/978-1-60327-241-4_18

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  • DOI: https://doi.org/10.1007/978-1-60327-241-4_18

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  • Publisher Name: Humana Press

  • Print ISBN: 978-1-60327-240-7

  • Online ISBN: 978-1-60327-241-4

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