White Rose University Consortium logo
University of Leeds logo University of Sheffield logo York University logo

Coarse-grained model of entropic allostery

Hawkins, R.J. and McLeish, T.C.B. (2004) Coarse-grained model of entropic allostery. Physical Review Letters, 93 (9). Art. No. 098104. ISSN 0031-9007

Full text available as:
[img]
Preview
Text
mcleishtcb10.pdf
Available under licence : See the attached licence file.

Download (201Kb)

Abstract

Many signaling functions in molecular biology require proteins to bind to substrates such as DNA in response to environmental signals such as the simultaneous binding to a small molecule. Examples are repressor proteins which may transmit information via a conformational change in response to the ligand binding. An alternative entropic mechanism of "allostery" suggests that the inducer ligand changes the intramolecular vibrational entropy, not just the mean static structure. We present a quantitative, coarse-grained model of entropic allostery, which suggests design rules for internal cohesive potentials in proteins employing this effect. It also addresses the issue of how the signal information to bind or unbind is transmitted through the protein. The model may be applicable to a wide range of repressors and also to signaling in trans-membrane proteins.

Item Type: Article
Copyright, Publisher and Additional Information: © 2004 The American Physical Society. Reproduced in accordance with the publisher's self-archiving policy.
Institution: The University of Leeds
Academic Units: The University of Leeds > Faculty of Maths and Physical Sciences (Leeds) > School of Physics and Astronomy (Leeds)
The University of Leeds > University of Leeds Research Centres and Institutes > Interdisciplinary Research Centre in Polymer Science and Technology (Leeds)
Depositing User: Repository Officer
Date Deposited: 17 Aug 2006
Last Modified: 05 Jun 2014 01:10
Published Version: http://link.aps.org/abstract/PRL/v93/e098104
Status: Published
Publisher: American Physical Society
Refereed: Yes
Identification Number: 10.1103/PhysRevLett.93.098104
URI: http://eprints.whiterose.ac.uk/id/eprint/1509

Actions (login required)

View Item View Item