The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Forces contributing to the conformational stability of proteins
Abstract
For 35 years, the prevailing view has been that the hydrophobic effect is the dominant force in protein folding. The importance of hydrogen bonding was always clear, but whether it made a net favorable contribution to protein stability was not. Studies of mutant proteins have improved our understanding of the forces stabilizing proteins. They suggest that hydrogen bonding and the hydrophobic effect make large but comparable contributions to the stability of globular proteins.—Pace, C. N., Shirley, B. A., McNutt, M., Gajiwala, K. Forces contributing to the conformational stability of proteins. FASEB J. 10, 75‐83 (1996)
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Blaber, M., Lindstrom, J. D., Gassner, N., Xu, J., Heinz, D. W., & Matthews, B. W. (1993) · Biochemistry · doi:10.1021/bi00093a013 · Cited by 93
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Chi, E. Y., Krishnan, S., Randolph, T. W., & Carpenter, J. F. (2003) · Pharmaceutical Research · doi:10.1023/a:1025771421906 · Cited by 1,379
Ageing and vision: structure, stability and function of lens crystallins
Bloemendal, H., de Jong, W., Jaenicke, R., Lubsen, N. H., Slingsby, C., & Tardieu, A. (2004) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2003.11.012 · Cited by 853
Experimental Binding Energies in Supramolecular Complexes
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Metadata
- Authors
- Pace, C. N., Shirley, B. A., McNutt, M., & Gajiwala, K.
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 1996-01
- Volume
- 10
- Issue
- 1
- Pages
- 75-83
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W1931164952
- Cited by
- 650
- References
- 1
- FWCI
- 5.44
- Type
- journal article
- Language
- en
- Open access
- closed
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- Pace, C. N., Shirley, B. A., McNutt, M., & Gajiwala, K. (1996). Forces contributing to the conformational stability of proteins. The FASEB Journal. https://doi.org/10.1096/fasebj.10.1.8566551
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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.
