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Versatility from Protein Disorder

Published:2012-09-21 Issue:6101 Volume:337 Page:1460-1461
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Babu M. Madan¹,Kriwacki Richard W.²,Pappu Rohit V.³

Affiliation:

1. MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK.

2. Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.

3. Department of Biomedical Engineering, Washington University of St Louis, St. Louis, MO 63130, USA.

Abstract

Synergy between disordered regions and structured domains increases the functional versatility of proteins and their interaction networks.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference16 articles.

1. Evolution of the Protein Repertoire

2. Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling

3. Intrinsically unstructured proteins and their functions

4. Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions

5. A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures

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