Format

Send to

Choose Destination
See comment in PubMed Commons below
Brief Bioinform. 2010 Mar;11(2):225-43. doi: 10.1093/bib/bbp061. Epub 2009 Dec 10.

Bioinformatical approaches to characterize intrinsically disordered/unstructured proteins.

Author information

1
Institute of Enzymology, H-1518 Budapest, Hungary.

Abstract

Intrinsically disordered/unstructured proteins exist without a stable three-dimensional (3D) structure as highly flexible conformational ensembles. The available genome sequences revealed that these proteins are surprisingly common and their frequency reaches high proportions in eukaryotes. Due to their vital role in various biological processes including signaling and regulation and their involvement in various diseases, disordered proteins and protein segments are the focus of many biochemical, molecular biological, pathological and pharmaceutical studies. These proteins are difficult to study experimentally because of the lack of unique structure in the isolated form. Their amino acid sequence, however, is available, and can be used for their identification and characterization by bioinformatic tools, analogously to globular proteins. In this review, we first present a small survey of current methods to identify disordered proteins or protein segments, focusing on those that are publicly available as web servers. In more detail we also discuss approaches that predict disordered regions and specific regions involved in protein binding by modeling the physical background of protein disorder. In our review we argue that the heterogeneity of disordered segments needs to be taken into account for a better understanding of protein disorder.

PMID:
20007729
DOI:
10.1093/bib/bbp061
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Silverchair Information Systems
    Loading ...
    Support Center