The DOI matches its Crossref record.
Hydrophobicity at Small and Large Length Scales
Open accessAbstract
We develop a unified and generally applicable theory of solvation of small and large apolar species in water. In the former, hydrogen bonding of water is hindered yet persists near the solutes. In the latter, hydrogen bonding is depleted, leading to drying of extended apolar surfaces, large forces of attraction, and hysteresis on mesoscopic length scales. The crossover occurs on nanometer length scales, when the local concentration of apolar units is sufficiently high, or when an apolar surface is sufficiently large. Our theory for the crossover has implications concerning the stability of protein assemblies and 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
Cited by
Friesner, R. A., Banks, J. L., Murphy, R. B., Halgren, T. A., Klicic, J. J., Mainz, D. T., Repasky, M. P., Knoll, E. H., Shelley, M., Perry, J. K., et al. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm0306430 · Cited by 10,057
g_mmpbsa—A GROMACS Tool for High-Throughput MM-PBSA Calculations
Kumari, R., Kumar, R., Open Source Drug Discovery Consortium, & Lynn, A. (2014) · Journal of Chemical Information and Modeling · doi:10.1021/ci500020m · Cited by 4,882
Water as an active constituent in cell biology
Ball, P. (2008) · Chemical Reviews · doi:10.1021/cr068037a · Cited by 2,177
Nature-inspired superwettability systems
Liu, M., Wang, S., & Jiang, L. (2017) · Nature Reviews Materials · doi:10.1038/natrevmats.2017.36 · Cited by 1,726
WATER MEDIATION IN PROTEIN FOLDING AND MOLECULAR RECOGNITION
Levy, Y., & Onuchic, J. N. (2006) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.35.040405.102134 · Cited by 1,048
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
Piana, S., Donchev, A. G., Robustelli, P., & Shaw, D. E. (2015) · The Journal of Physical Chemistry B · doi:10.1021/jp508971m · Cited by 852
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
How Water’s Properties Are Encoded in Its Molecular Structure and Energies
Brini, E., Fennell, C. J., Fernandez-Serra, M., Hribar-Lee, B., Lukšič, M., & Dill, K. A. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00259 · Cited by 518
Torquato, S. (2018) · Physics Reports · doi:10.1016/j.physrep.2018.03.001 · Cited by 499
Water is an active matrix of life for cell and molecular biology
Ball, P. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1703781114 · Cited by 484
Instantaneous Liquid Interfaces
Willard, A. P., & Chandler, D. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp909219k · Cited by 462
Self-citationThermal Conductance of Hydrophilic and Hydrophobic Interfaces
Ge, Z., Cahill, D. G., & Braun, P. V. (2006) · Physical Review Letters · doi:10.1103/physrevlett.96.186101 · Cited by 455
Reaction coordinates of biomolecular isomerization
Bolhuis, P. G., Dellago, C., & Chandler, D. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.100127697 · Cited by 426
Self-citationBall, P. (2008) · Nature · doi:10.1038/452291a · Cited by 384
Observation of a dewetting transition in the collapse of the melittin tetramer
Liu, P., Huang, X., Zhou, R., & Berne, B. J. (2005) · Nature · doi:10.1038/nature03926 · Cited by 373
Godawat, R., Jamadagni, S. N., & Garde, S. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902778106 · Cited by 357
Snyder, P. W., Mecinović, J., Moustakas, D. T., Thomas, S. W., Harder, M., Mack, E. T., Lockett, M. R., Héroux, A., Sherman, W., & Whitesides, G. M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1114107108 · Cited by 357
Gallicchio, E., & Levy, R. M. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.10400 · Cited by 328
Understanding β-hairpin formation
Dinner, A. R., Lazaridis, T., & Karplus, M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.16.9068 · Cited by 326
Ferreiro, D. U., Komives, E. A., & Wolynes, P. G. (2014) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583514000092 · Cited by 314
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
Water in Cavity−Ligand Recognition
Baron, R., Setny, P., & McCammon, J. A. (2010) · Journal of the American Chemical Society · doi:10.1021/ja1050082 · Cited by 274
Efficient Determination of Protein–Protein Standard Binding Free Energies from First Principles
Gumbart, J. C., Roux, B., & Chipot, C. (2013) · Journal of Chemical Theory and Computation · doi:10.1021/ct400273t · Cited by 211
Temperature-dependent solvation modulates the dimensions of disordered proteins
Wuttke, R., Hofmann, H., Nettels, D., Borgia, M. B., Mittal, J., Best, R. B., & Schuler, B. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1313006111 · Cited by 192
Systematic determination of order parameters for chain dynamics using diffusion maps
Ferguson, A. L., Panagiotopoulos, A. Z., Debenedetti, P. G., & Kevrekidis, I. G. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1003293107 · Cited by 165
The Hydrophobic Temperature Dependence of Amino Acids Directly Calculated from Protein Structures
van Dijk, E., Hoogeveen, A., & Abeln, S. (2015) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1004277 · Cited by 162
“Note that the correction to a reference of polar and charged amino acids was also performed in the resampling procedure to obtain statistical significance Fig 4 also shows that the estimated transfer free energies show a very similar trend with respect to temperature to those that have been measured for hydrophobic pa…”
MethodGiovambattista, N., Rossky, P. J., & Debenedetti, P. G. (2012) · Annual Review of Physical Chemistry · doi:10.1146/annurev-physchem-032811-112007 · Cited by 149
Functional Biochar Synergistic Solid/Liquid-Phase CO2 Capture: A Review
Zhang, Y., Wang, S., Feng, D., Gao, J., Dong, L., Zhao, Y., Sun, S., Huang, Y., & Qin, Y. (2022) · Energy & Fuels · doi:10.1021/acs.energyfuels.1c04372 · Cited by 91
Water Confinement in Hydrophobic Nanopores. Pressure-Induced Wetting and Drying
Smirnov, S., Vlassiouk, I., Takmakov, P., & Rios, F. (2010) · ACS Nano · doi:10.1021/nn101080k · Cited by 77
Mansbach, R. A., & Ferguson, A. L. (2015) · The Journal of Chemical Physics · doi:10.1063/1.4914144 · Cited by 39
Metadata
- Authors
- Lum, K., Chandler, D., & Weeks, J. D.
- Venue
- The Journal of Physical Chemistry B
- Publisher
- American Chemical Society (ACS)
- Published
- 1999-04-16
- Volume
- 103
- Issue
- 22
- Pages
- 4570-4577
- ISSN
- 1520-5207 (ISSN-L)
- 1520-6106
- OpenAlex
- W2131754023
- Cited by
- 1,670
- References
- 0
- FWCI
- 27.83
- Type
- journal article
- Language
- en
- Open access
- bronze
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
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.
