The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.
On the Mechanism of Hydrophobic Association of Nanoscopic Solutes
Abstract
The hydration behavior of two planar nanoscopic hydrophobic solutes in liquid water at normal temperature and pressure is investigated by calculating the potential of mean force between them at constant pressure as a function of the solute-solvent interaction potential. The importance of the effect of weak attractive interactions between the solute atoms and the solvent on the hydration behavior is clearly demonstrated. We focus on the underlying mechanism behind the contrasting results obtained in various recent experimental and computational studies on water near hydrophobic solutes. The length scale where crossover from a solvent separated state to the contact pair state occurs is shown to depend on the solute sizes as well as on details of the solute-solvent interaction. We find the mechanism for attractive mean forces between the plates is very different depending on the nature of the solute-solvent interaction which has implications for the mechanism of the hydrophobic effect for biomolecules.
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Cites
Computer Simulation of Liquids
P, S., & J, K. (1988) · Journal of Molecular Liquids · doi:10.1016/0167-7322(88)80022-9 · Cited by 15,812
The missing term in effective pair potentials
Berendsen, H. J. C., Grigera, J. R., & Straatsma, T. P. (1987) · The Journal of Physical Chemistry · doi:10.1021/j100308a038 · Cited by 13,345
A Second Generation Force Field for the Simulation of Proteins, Nucleic Acids, and Organic Molecules
Cornell, W. D., Cieplak, P., Bayly, C. I., Gould, I. R., Merz, K. M., Ferguson, D. M., Spellmeyer, D. C., Fox, T., Caldwell, J. W., & Kollman, P. A. (1995) · Journal of the American Chemical Society · doi:10.1021/ja00124a002 · Cited by 13,103
Molecular dynamics simulations at constant pressure and/or temperature
Andersen, H. C. (1980) · The Journal of Chemical Physics · doi:10.1063/1.439486 · Cited by 5,758
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
Swope, W. C., Andersen, H. C., Berens, P. H., & Wilson, K. R. (1982) · The Journal of Chemical Physics · doi:10.1063/1.442716 · Cited by 4,051
Dominant forces in protein folding
Dill, K. A. (1990) · Biochemistry · doi:10.1021/bi00483a001 · Cited by 3,800
Water conduction through the hydrophobic channel of a carbon nanotube
Hummer, G., Rasaiah, J. C., & Noworyta, J. P. (2001) · Nature · doi:10.1038/35102535 · Cited by 3,557
Constant pressure molecular dynamics for molecular systems
Nosé, S., & Klein, M. L. (1983) · Molecular Physics · doi:10.1080/00268978300102851 · Cited by 3,260
Rattle: A “velocity” version of the shake algorithm for molecular dynamics calculations
Andersen, H. C. (1983) · Journal of Computational Physics · doi:10.1016/0021-9991(83)90014-1 · Cited by 3,081
Cited by
Water as an active constituent in cell biology
Ball, P. (2008) · Chemical Reviews · doi:10.1021/cr068037a · Cited by 2,177
Shih, C.-J., Lin, S., Sharma, R., Strano, M. S., & Blankschtein, D. (2012) · Langmuir · doi:10.1021/la203607w · Cited by 605
Giovambattista, N., Rossky, P. J., & Debenedetti, P. G. (2006) · Physical Review E · doi:10.1103/physreve.73.041604 · Cited by 358
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
- Choudhury, N., & Pettitt, B. M.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2005-02-19
- Volume
- 127
- Issue
- 10
- Pages
- 3556-3567
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2000894690
- Cited by
- 292
- References
- 52
- FWCI
- 13.14
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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