Format

Send to

Choose Destination
See comment in PubMed Commons below
Arch Biochem Biophys. 2012 Aug 15;524(2):123-31. doi: 10.1016/j.abb.2012.04.024. Epub 2012 May 9.

Towards the physical basis of how intrinsic disorder mediates protein function.

Author information

1
Department of Biochemistry, Kansas State University, Manhattan, KS 66506, USA. jianhanc@ksu.edu

Abstract

Intrinsically disordered proteins (IDPs) are an important class of functional proteins that is highly prevalent in biology and has broad association with human diseases. In contrast to structured proteins, free IDPs exist as heterogeneous and dynamical conformational ensembles under physiological conditions. Many concepts have been discussed on how such intrinsic disorder may provide crucial functional advantages, particularly in cellular signaling and regulation. Establishing the physical basis of these proposed phenomena requires not only detailed characterization of the disordered conformational ensembles, but also mechanistic understanding of the roles of various ensemble properties in IDP interaction and regulation. Here, we review the experimental and computational approaches that may be integrated to address many important challenges of establishing a "structural" basis of IDP function, and discuss some of the key emerging ideas on how the conformational ensembles of IDPs may mediate function, especially in coupled binding and folding interactions.

PMID:
22579883
DOI:
10.1016/j.abb.2012.04.024
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Support Center