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J Am Chem Soc. 2011 Aug 3;133(30):11515-23. doi: 10.1021/ja1098287. Epub 2011 Jul 7.

A multidisciplinary approach to probing enthalpy-entropy compensation and the interfacial mobility model.

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  • 1Department of Chemistry, Duke University, Durham, North Carolina 27708, USA.

Abstract

In recent years, interfacial mobility has gained popularity as a model with which to rationalize both affinity in ligand binding and the often observed phenomenon of enthalpy-entropy compensation. While protein contraction and reduced mobility, as demonstrated by computational and NMR techniques respectively, have been correlated to entropies of binding for a variety of systems, to our knowledge, Raman difference spectroscopy has never been included in these analyses. Here, nonresonance Raman difference spectroscopy, isothermal titration calorimetry, and X-ray crystallography were utilized to correlate protein contraction, as demonstrated by an increase in protein interior packing and decreased residual protein movement, with trends of enthalpy-entropy compensation. These results are in accord with the interfacial mobility model and lend additional credence to this view of protein activity.

PMID:
21692482
[PubMed - indexed for MEDLINE]
PMCID:
PMC3151494
Free PMC Article
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