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Editorial
. 2020 Jan 13;21(2):504.
doi: 10.3390/ijms21020504.

Macromolecular Interactions of Disordered Proteins

István Simon  1
Affiliations
Editorial

Macromolecular Interactions of Disordered Proteins

István Simon. Int J Mol Sci. .

Abstract

Proteins are social beings [...].

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Conflict of interest statement

The author declares no conflict of interest.

References

    1. Wright P.E., Dyson H.J. Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm. J. Mol. Biol. 1999;293:321–331. doi: 10.1006/jmbi.1999.3110. - DOI - PubMed
    1. Dosztányi Z., Csizmók V., Tompa P., Simon I. The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins. J. Mol. Biol. 2005;347:827–839. doi: 10.1016/j.jmb.2005.01.071. - DOI - PubMed
    1. Dosztanyi Z., Csizmok V., Tompa P., Simon I. IUPred: Web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics. 2005;21:3433–3434. doi: 10.1093/bioinformatics/bti541. - DOI - PubMed
    1. Mészáros B., Simon I., Dosztányi Z. Prediction of protein binding regions in disordered proteins. PLoS Comput. Biol. 2009;5:e1000376. - PMC - PubMed
    1. Dosztányi Z., Mészáros B., Simon I. ANCHOR: Web server for predicting protein binding regions in disordered proteins. Bioinformatics. 2009;25:2745–2746. doi: 10.1093/bioinformatics/btp518. - DOI - PMC - PubMed

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