The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
Temperature and length scale dependence of hydrophobic effects and their possible implications for protein folding
Open accessAbstract
The Lum–Chandler–Weeks theory of hydrophobicity [Lum, K., Chandler, D. & Weeks, J. D. (1999) J. Phys. Chem. 103, 4570–4577] is applied to treat the temperature dependence of hydrophobic solvation in water. The application illustrates how the temperature dependence for hydrophobic surfaces extending less than 1 nm differs significantly from that for surfaces extending more than 1 nm. The latter is the result of water depletion, a collective effect, that appears at length scales of 1 nm and larger. Because of the contrasting behaviors at small and large length scales, hydrophobicity by itself can explain the variable behavior of entropies of protein folding.
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
Cites
CRC Handbook of Chemistry and Physics
(2014) · doi:10.1201/b17118 · Cited by 57,706
CRC Handbook of Chemistry and Physics
(2016) · CRC Press eBooks · doi:10.1201/9781315380476 · Cited by 13,921
Some Factors in the Interpretation of Protein Denaturation
Kauzmann, W. (1959) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60608-7 · Cited by 4,870
The Hydrophobic Effect: Formation of Micelles and Biological Membranes
Tanford, C. (1991) · Medical Entomology and Zoology · Cited by 3,327
Hydrophobicity at Small and Large Length Scales
Lum, K., Chandler, D., & Weeks, J. D. (1999) · The Journal of Physical Chemistry B · doi:10.1021/jp984327m · Cited by 1,670
Self-citationPrivalov, P. L., & Khechinashvili, N. N. (1974) · Journal of Molecular Biology · doi:10.1016/0022-2836(74)90188-0 · Cited by 1,399
Stability of Protein Structure and Hydrophobic Interaction
Privalov, P. L., & Gill, S. J. (1988) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60377-0 · Cited by 1,303
Energetics of Protein Structure
(1995) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60548-3 · Cited by 1,065
Temperature dependence of the hydrophobic interaction in protein folding.
Baldwin, R. L. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.21.8069 · Cited by 893
Theory of the hydrophobic effect
Pratt, L. R., & Chandler, D. (1977) · The Journal of Chemical Physics · doi:10.1063/1.435308 · Cited by 827
Self-citation
Cited by
A View of the Hydrophobic Effect
Southall, N. T., Dill, K. A., & Haymet, A. D. J. (2002) · The Journal of Physical Chemistry B · doi:10.1021/jp015514e · Cited by 913
Hydrophobic Collapse in Multidomain Protein Folding
Zhou, R., Huang, X., Margulis, C. J., & Berne, B. J. (2004) · Science · doi:10.1126/science.1101176 · Cited by 511
Prabhu, N. V., & Sharp, K. A. (2005) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.56.092503.141202 · Cited by 425
Wagoner, J. A., & Baker, N. A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600118103 · Cited by 310
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
Metadata
- Authors
- Huang, D. M., & Chandler, D.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2000-07-11
- Volume
- 97
- Issue
- 15
- Pages
- 8324-8327
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2057431120
- Cited by
- 379
- References
- 25
- FWCI
- 2.93
- 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: Temperature and length scale dependence of hydrophobic effects and their possible implications for protein folding. https://app.cochat.ai/papers/10.1073/pnas.120176397
- The paper
- Huang, D. M., & Chandler, D. (2000). Temperature and length scale dependence of hydrophobic effects and their possible implications for protein folding. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.120176397
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.
