The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins
Open accessAbstract
Proteins can be denatured by pressures of a few hundred MPa. This finding apparently contradicts the most widely used model of protein stability, where the formation of a hydrophobic core drives protein folding. The pressure denaturation puzzle is resolved by focusing on the pressure-dependent transfer of water into the protein interior, in contrast to the transfer of nonpolar residues into water, the approach commonly taken in models of protein unfolding. Pressure denaturation of proteins can then be explained by the pressure destabilization of hydrophobic aggregates by using an information theory model of hydrophobic interactions. Pressure-denatured proteins, unlike heat-denatured proteins, retain a compact structure with water molecules penetrating their core. Activation volumes for hydrophobic contributions to protein folding and unfolding kinetics are positive. Clathrate hydrates are predicted to form by virtually the same mechanism that drives pressure denaturation of proteins.
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Cites
Funnels, pathways, and the energy landscape of protein folding: A synthesis
Bryngelson, J. D., Onuchic, J. N., Socci, N. D., & Wolynes, P. G. (1995) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340210302 · Cited by 2,648
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
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
Godawat, R., Jamadagni, S. N., & Garde, S. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902778106 · Cited by 357
Self-citationGiovambattista, N., Rossky, P. J., & Debenedetti, P. G. (2012) · Annual Review of Physical Chemistry · doi:10.1146/annurev-physchem-032811-112007 · Cited by 149
Solute accumulation in the deep-sea bacterium Photobacterium profundum
Martin, D., Bartlett, D., & Roberts, M. (2002) · Extremophiles · doi:10.1007/s00792-002-0288-1 · Cited by 133
Metadata
- Authors
- Hummer, G., Garde, S., García, A. E., Paulaitis, M. E., & Pratt, L. R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1998-02-17
- Volume
- 95
- Issue
- 4
- Pages
- 1552-1555
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1974137193
- Cited by
- 591
- References
- 1
- FWCI
- 7.99
- Type
- journal article
- Language
- en
- Open access
- green
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- Hummer, G., Garde, S., García, A. E., Paulaitis, M. E., & Pratt, L. R. (1998). The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.95.4.1552
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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.
