The DOI matches its Crossref record; 59 of the 59 references it cites were found in a registry or an index.
Free Energy Balance in Protein Folding
Open accessAbstract
This chapter suggests a particular decomposition that relies on classical concepts and that is intuitively straightforward. It aims to provide a semi-quantitative basis for the interpretation of experiments. These include thermodynamic studies of the entire folding process, experiments based on site-directed mutagenesis that attempt to isolate the free energy contributions of individual groups and studies of folding intermediates. A fundamental problem in any attempt at analysis is that the free energy change associated with protein folding is usually described in terms of forces that are much larger than their resultant. The chapter aims to arrive at a model capable of accounting for the small free energy changes that accompany protein folding while providing a more quantitative description of the effects of single-site mutations. The approach is to characterize individual forces by extracting information as to their magnitudes from direct measurements on proteins, from the principles of physical chemistry, and from the methods of continuum electrostatics. The relevant theory and experimental data are discussed individually and an attempt has been made to extract some general principles about protein folding.
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Cites
Nicholls, A., Sharp, K. A., & Honig, B. (1991) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340110407 · Cited by 5,240
Thermodynamics of High Polymer Solutions
Flory, P. J. (1942) · The Journal of Chemical Physics · doi:10.1063/1.1723621 · Cited by 4,374
Dominant forces in protein folding
Dill, K. A. (1990) · Biochemistry · doi:10.1021/bi00483a001 · Cited by 3,800
Semianalytical treatment of solvation for molecular mechanics and dynamics
Still, W. C., Tempczyk, A., Hawley, R. C., & Hendrickson, T. (1990) · Journal of the American Chemical Society · doi:10.1021/ja00172a038 · Cited by 3,643
Solutions of Long Chain Compounds
Huggins, M. L. (1941) · The Journal of Chemical Physics · doi:10.1063/1.1750930 · Cited by 1,919
Thermodynamics of High Polymer Solutions
Flory, P. J. (1941) · The Journal of Chemical Physics · doi:10.1063/1.1750971 · Cited by 1,447
Kuwajima, K. (1989) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340060202 · Cited by 1,439
Stability of Protein Structure and Hydrophobic Interaction
Privalov, P. L., & Gill, S. J. (1988) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60377-0 · Cited by 1,303
pKa's of ionizable groups in proteins: atomic detail from a continuum electrostatic model
Bashford, D., & Karplus, M. (1990) · Biochemistry · doi:10.1021/bi00496a010 · Cited by 1,083
Hydrogen bonding and biological specificity analysed by protein engineering
Fersht, A. R., Shi, J.-P., Knill-Jones, J., Lowe, D. M., Wilkinson, A. J., Blow, D. M., Brick, P., Carter, P., Waye, M. M. Y., & Winter, G. (1985) · Nature · doi:10.1038/314235a0 · Cited by 1,056
Cited by
Intrinsically disordered protein
Dunker, A. K., Lawson, J. D., Brown, C. J., Williams, R. M., Romero, P., Oh, J. S., Oldfield, C. J., Campen, A. M., Ratliff, C. M., Hipps, K. W., et al. (2001) · Journal of Molecular Graphics and Modelling · doi:10.1016/s1093-3263(00)00138-8 · Cited by 2,272
Gallicchio, E., & Levy, R. M. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.10400 · Cited by 328
Hydrogen bonding stabilizes globular proteins
Myers, J. K., & Pace, C. N. (1996) · Biophysical Journal · doi:10.1016/s0006-3495(96)79401-8 · Cited by 308
Metadata
- Venue
- Advances in Protein Chemistry
- Publisher
- Elsevier
- Published
- 1995
- Volume
- 46
- Pages
- 27-58
- ISSN
- 0065-3233 (ISSN-L)
- OpenAlex
- W1537016059
- Cited by
- 275
- References
- 59
- FWCI
- 25.15
- Type
- book chapter
- Language
- en
- Open access
- hybrid
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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