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Predicting the energetics of osmolyte-induced protein folding/unfolding
Open accessAbstract
A primary thermodynamic goal in protein biochemistry is to attain predictive understanding of the detailed energetic changes that are responsible for folding/unfolding. Through use of recently determined free energies of side-chain and backbone transfer from water to osmolytes and Tanford's transfer model, we demonstrate that the long-sought goal of predicting solvent-dependent cooperative protein folding/unfolding free-energy changes ( m values) can be achieved. Moreover, the approach permits dissection of the folding/unfolding free-energy changes into individual contributions from the peptide backbone and residue side chains.
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Cited by
A molecular mechanism for osmolyte-induced protein stability
Street, T. O., Bolen, D. W., & Rose, G. D. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606236103 · Cited by 667
Self-citationTherapeutic protein aggregation: mechanisms, design, and control
Roberts, C. J. (2014) · Trends in Biotechnology · doi:10.1016/j.tibtech.2014.05.005 · Cited by 455
Structure and Energetics of the Hydrogen-Bonded Backbone in Protein Folding
Bolen, D. W., & Rose, G. D. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.061306.131357 · Cited by 408
Self-citationInhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant
Ignatova, Z., & Gierasch, L. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603772103 · Cited by 320
Coil–globule transition in the denatured state of a small protein
Sherman, E., & Haran, G. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601395103 · Cited by 294
Metadata
- Authors
- Auton, M., & Bolen, D. W.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2005-10-07
- Volume
- 102
- Issue
- 42
- Pages
- 15065-15068
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2096409300
- Cited by
- 433
- References
- 0
- FWCI
- 8.30
- Type
- journal article
- Language
- en
- Open access
- green
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