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Bioinformatical Approaches to Unstructured/Disordered Proteins and Their Interactions

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Computational Methods to Study the Structure and Dynamics of Biomolecules and Biomolecular Processes

Part of the book series: Springer Series in Bio-/Neuroinformatics ((SSBN,volume 1))

Abstract

Intrinsically unstructured/disordered proteins (IUPs/IDPs) exist as highly flexible conformational ensembles without adopting a stable three-dimensional structure. Experimental and bioinformatical studies in the past two decades have shown that these proteins play a central role in various signaling and regulatory processes. Accordingly, their frequency in higher eukaryotes reaches high proportions and their malfunction can be connected to a wide variety of diseases. Recognizing the biological importance of these proteins motivated researchers to understand various aspects of disordered proteins and protein segments from the viewpoint of biochemistry, molecular biology and pharmacology. In general, IDPs are difficult to study experimentally because of the lack of a unique structure in the isolated form. Nevertheless, various bioinformatics tools developed over the last few years enable their identification and characterization using only the amino acid sequence. In this chapter — after a brief introduction to IDPs in general — we present a small survey of current methods aimed at identifying disordered proteins or protein segments, focusing on those that are publicly available as web servers. We also discuss in more detail approaches that predict disordered regions and specific regions involved in protein binding by modeling the physical background of protein disorder. Furthermore, we argue that the heterogeneity of disordered segments needs to be taken into account for a better understanding of protein disorder and the correct use and interpretation of the output of disorder prediction algorithms.

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Authors and Affiliations

  1. Institute of Enzymology, RCNS, HAS, Budapest, Hungary

    Bálint Mészáros, Zsuzsanna Dosztányi, Csaba Magyar & István Simon

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  1. Bálint Mészáros
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  2. Zsuzsanna Dosztányi
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  3. Csaba Magyar
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  4. István Simon
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Correspondence to Bálint Mészáros .

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  1. , Faculty of Chemistry, University of Gdansk, Sobieskiego 18, Gdansk, 80-952, Poland

    Adam Liwo

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Mészáros, B., Dosztányi, Z., Magyar, C., Simon, I. (2014). Bioinformatical Approaches to Unstructured/Disordered Proteins and Their Interactions. In: Liwo, A. (eds) Computational Methods to Study the Structure and Dynamics of Biomolecules and Biomolecular Processes. Springer Series in Bio-/Neuroinformatics, vol 1. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-28554-7_16

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