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

Journal Article (Journal Article)

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.

Full Text

Duke Authors

Cited Authors

  • Wilfong, EM; Kogiso, Y; Muthukrishnan, S; Kowatz, T; Du, Y; Bowie, A; Naismith, JH; Hadad, CM; Toone, EJ; Gustafson, TL

Published Date

  • August 2011

Published In

Volume / Issue

  • 133 / 30

Start / End Page

  • 11515 - 11523

PubMed ID

  • 21692482

Pubmed Central ID

  • PMC3151494

Electronic International Standard Serial Number (EISSN)

  • 1520-5126

International Standard Serial Number (ISSN)

  • 0002-7863

Digital Object Identifier (DOI)

  • 10.1021/ja1098287


  • eng