The DOI matches its Crossref record.
Origin of Entropy Convergence in Hydrophobic Hydration and Protein Folding
Open accessAbstract
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cited by
Water as an active constituent in cell biology
Ball, P. (2008) · Chemical Reviews · doi:10.1021/cr068037a · Cited by 2,177
Water structural transformation at molecular hydrophobic interfaces
Davis, J. G., Gierszal, K. P., Wang, P., & Ben-Amotz, D. (2012) · Nature · doi:10.1038/nature11570 · Cited by 587
Hydrophobic hydration from small to large lengthscales: Understanding and manipulating the crossover
Rajamani, S., Truskett, T. M., & Garde, S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504089102 · Cited by 300
Self-citation
Metadata
- Authors
- Garde, S., Hummer, G., García, A. E., Paulaitis, M. E., & Pratt, L. R.
- Venue
- Physical Review Letters
- Publisher
- American Physical Society (APS)
- 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Origin of Entropy Convergence in Hydrophobic Hydration and Protein Folding. https://app.cochat.ai/papers/10.1103/physrevlett.77.4966
- The paper
- 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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.