The ensemble nature of allostery
Hesam N. Motlagh,
James O. Wrabl,
Jing Li and
Vincent J. Hilser ()
Additional contact information
Hesam N. Motlagh: Johns Hopkins University
James O. Wrabl: Johns Hopkins University
Jing Li: Johns Hopkins University
Vincent J. Hilser: Johns Hopkins University
Nature, 2014, vol. 508, issue 7496, 331-339
Abstract:
Allostery is the process by which biological macromolecules transmit the effect of binding at one site to another, often distal, functional site, allowing for the regulation of activity; here facilitation of allostery through dynamic and intrinsically disordered proteins is discussed, and a framework to unify the description of allosteric mechanisms for different systems is proposed.
Date: 2014
References: Add references at CitEc
Citations: View citations in EconPapers (15)
Downloads: (external link)
https://www.nature.com/articles/nature13001 Abstract (text/html)
Access to the full text of the articles in this series is restricted.
Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.
Export reference: BibTeX
RIS (EndNote, ProCite, RefMan)
HTML/Text
Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:508:y:2014:i:7496:d:10.1038_nature13001
Ordering information: This journal article can be ordered from
https://www.nature.com/
DOI: 10.1038/nature13001
Access Statistics for this article
Nature is currently edited by Magdalena Skipper
More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().