Conformational entropy in molecular recognition by proteins

Kendra King Frederick, Michael S. Marlow, Kathleen G. Valentine and A. Joshua Wand ()
Additional contact information
Kendra King Frederick: University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA
Michael S. Marlow: University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA
Kathleen G. Valentine: University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA
A. Joshua Wand: University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA

Nature, 2007, vol. 448, issue 7151, 325-329

Abstract: Abstract Molecular recognition by proteins is fundamental to almost every biological process, particularly the protein associations underlying cellular signal transduction. Understanding the basis for protein–protein interactions requires the full characterization of the thermodynamics of their association. Historically it has been virtually impossible to experimentally estimate changes in protein conformational entropy, a potentially important component of the free energy of protein association. However, nuclear magnetic resonance spectroscopy has emerged as a powerful tool for characterizing the dynamics of proteins. Here we employ changes in conformational dynamics as a proxy for corresponding changes in conformational entropy. We find that the change in internal dynamics of the protein calmodulin varies significantly on binding a variety of target domains. Surprisingly, the apparent change in the corresponding conformational entropy is linearly related to the change in the overall binding entropy. This indicates that changes in protein conformational entropy can contribute significantly to the free energy of protein–ligand association.

Date: 2007
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/nature05959 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:448:y:2007:i:7151:d:10.1038_nature05959

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature05959

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 ().