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Hydrophobicity of Amino Acid Residues in Globular Proteins
Abstract
During biosynthesis, a globular protein folds into a tight particle with an interior core that is shielded from the surrounding solvent. The hydrophobic effect is thought to play a key role in mediating this process: nonpolar residues expelled from water engender a molecular interior where they can be buried. Paradoxically, results of earlier quantitative analyses have suggested that the tendency for nonpolar residues to be buried within proteins is weak. However, such analyses merely classify residues as either "exposed" or "buried." In the experiment reported in this article proteins of known structure were used to measure the average area that each residue buries upon folding. This characteristic quantity, the average area buried, is correlated with residue hydrophobicity.
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Cites
The Hydrophobic Effect and the Organization of Living Matter
Tanford, C. (1978) · Science · doi:10.1126/science.653353 · Cited by 985
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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
Accessible surface areas as a measure of the thermodynamic parameters of hydration of peptides.
Ooi, T., Oobatake, M., Némethy, G., & Scheraga, H. A. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.10.3086 · Cited by 746
Collawn, J. F., Stangel, M., Kuhn, L. A., Esekogwu, V., Jing, S., Trowbridge, I. S., & Tainer, J. A. (1990) · Cell · doi:10.1016/0092-8674(90)90509-d · Cited by 518
CAMP: a useful resource for research on antimicrobial peptides.
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Metadata
- Authors
- Rose, G. D., Geselowitz, A. R., Lesser, G. J., Lee, R. H., & Zehfus, M. H.
- Venue
- Science
- Published
- 1985-08-30
- Volume
- 229
- Issue
- 4716
- Pages
- 834-838
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1997870466
- Cited by
- 1,175
- References
- 1
- FWCI
- 10.80
- Type
- journal article
- Language
- en
- Open access
- closed
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- Rose, G. D., Geselowitz, A. R., Lesser, G. J., Lee, R. H., & Zehfus, M. H. (1985). Hydrophobicity of Amino Acid Residues in Globular Proteins. Science. https://doi.org/10.1126/science.4023714
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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.
