The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
Heat capacity and entropy changes in processes involving proteins.
Open accessAbstract
Six possible sources of the large heat capacity and entropy changes frequently observed for processes involving proteins are identified. Of these the conformational, hydrophobic, and vibrational effects seem likely to be of greatest importance. A method is proposed for estimating the magnitudes of the hydrophobic and vibrational contributions. Application of this method to several protein processes appears to achieve significant clarification of previously confusing and apparently contradictory data.
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Citations
Cites
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Cited by
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
The structure of protein-protein recognition sites.
Janin, J., & Chothia, C. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)46181-3 · Cited by 819
Structure and Flexibility Adaptation in Nonspecific and Specific Protein-DNA Complexes
Kalodimos, C. G., Biris, N., Bonvin, A. M. J. J., Levandoski, M. M., Guennuegues, M., Boelens, R., & Kaptein, R. (2004) · Science · doi:10.1126/science.1097064 · Cited by 543
Protein folding: local structures, domains, subunits, and assemblies
Jaenicke, R. (1991) · Biochemistry · doi:10.1021/bi00227a001 · Cited by 438
Gallicchio, E., & Levy, R. M. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.10400 · Cited by 328
Metadata
- Authors
- Sturtevant, J. M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1977-06
- Volume
- 74
- Issue
- 6
- Pages
- 2236-2240
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2021163287
- Cited by
- 855
- References
- 15
- FWCI
- 7.32
- Type
- journal article
- Language
- en
- Open access
- green
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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.
