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Cited by 261

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Origin of Entropy Convergence in Hydrophobic Hydration and Protein Folding

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Garde, Shekhar, Hummer, Gerhard, García, Angel E., Paulaitis, Michael E., Pratt, Lawrence R.·1996·Physical Review Letters

Abstract

An information theory model is used to construct a molecular explanation why hydrophobic solvation entropies measured in calorimetry of protein unfolding converge at a common temperature. The entropy convergence follows from the weak temperature dependence of occupancy fluctuations for molecular-scale volumes in water. The macroscopic expression of the contrasting entropic behavior between water and common organic solvents is the relative temperature insensitivity of the water isothermal compressibility. The information theory model provides a quantitative description of small molecule hydration and predicts a negative entropy at convergence. Interpretations of entropic contributions to protein folding should account for this result.

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Metadata

Authors
Garde, S., Hummer, G., García, A. E., Paulaitis, M. E., & Pratt, L. R.
Venue
Physical Review Letters
Published
1996-12-09
Volume
77
Issue
24
Pages
4966-4968
ISSN
  • 0031-9007 (ISSN-L)
  • 1079-7114
OpenAlex
W2085806783
Cited by
261
References
0
FWCI
3.96
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Origin of Entropy Convergence in Hydrophobic Hydration and Protein Folding. https://app.cochat.ai/papers/10.1103/physrevlett.77.4966
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Garde, S., Hummer, G., García, A. E., Paulaitis, M. E., & Pratt, L. R. (1996). Origin of Entropy Convergence in Hydrophobic Hydration and Protein Folding. Physical Review Letters. https://doi.org/10.1103/physrevlett.77.4966

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.