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Prediction and analysis of intrinsically disordered proteins.

TitlePrediction and analysis of intrinsically disordered proteins.
Publication TypeJournal Article
Year of Publication2015
AuthorsPunta, M, Simon, I, Dosztányi, Z
JournalMethods Mol Biol
Volume1261
Pagination35-59
Date Published2015
ISSN1940-6029
KeywordsCrystallography, Databases, Protein, Intrinsically Disordered Proteins, Protein Conformation, Proteomics
Abstract

Intrinsically disordered proteins and protein regions (IDPs/IDRs) do not adopt a well-defined folded structure under physiological conditions. Instead, these proteins exist as heterogeneous and dynamical conformational ensembles. IDPs are widespread in eukaryotic proteomes and are involved in fundamental biological processes, mostly related to regulation and signaling. At the same time, disordered regions often pose significant challenges to the structure determination process, which generally requires highly homogeneous proteins samples. In this book chapter, we provide a brief overview of protein disorder, describe various bioinformatics resources that have been developed in recent years for their characterization, and give a general outline of their applications in various types of structural genomics projects. Traditionally, disordered segments were filtered out to optimize the yield of structure determination pipelines. However, it is becoming increasingly clear that the structural characterization of proteins cannot be complete without the incorporation of intrinsically disordered regions.

DOI10.1007/978-1-4939-2230-7_3
Alternate JournalMethods Mol. Biol.
PubMed ID25502193
Grant ListWT077044/Z/05/Z / / Wellcome Trust / United Kingdom