The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Protein folding and binding in confined spaces and in crowded solutions
Open accessAbstract
Simple theoretical models are presented to illustrate the effects of spatial confinement and macromolecular crowding on the equilibria and rates of protein folding and binding. Confinement is expected to significantly stabilize the folded state, but for crowding only a marginal effect on protein stability is expected. In confinement the unfolded chain is restricted to a cage but in crowding the unfolded chain may explore different interstitial voids. Because confinement and crowding eliminate the more expanded conformations of the unfolded state, folding from the compact unfolded state is expected to speed up. Crowding will shift the binding equilibrium of proteins toward the bound state. The significant slowing down in protein diffusion by crowding, perhaps beneficial for chaperonin action, could result in a decrease in protein binding rates. Copyright © 2004 John Wiley & Sons, Ltd.
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Citations
Cites
Macromolecular crowding: obvious but underappreciated
Ellis, R. J. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01938-7 · Cited by 2,309
Implications of macromolecular crowding for protein assembly
Minton, A. P. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)00045-7 · Cited by 649
Molecular confinement influences protein structure and enhances thermal protein stability
Eggers, D. K., & Valentine, J. S. (2001) · Protein Science · doi:10.1110/ps.36201 · Cited by 393
Minton, A. P. (1998) · Methods in Enzymology · doi:10.1016/s0076-6879(98)95038-8 · Cited by 317
Minton, A. P. (2000) · Biophysical Journal · doi:10.1016/s0006-3495(00)76576-3 · Cited by 218
Tracer diffusion of globular proteins in concentrated protein solutions.
Muramatsu, N., & Minton, A. P. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.9.2984 · Cited by 178
Cited by
Peptide and Amide Bond-Containing Dendrimers
Crespo, L., Sanclimens, G., Pons, M., Giralt, E., Royo, M., & Albericio, F. (2005) · Chemical Reviews · doi:10.1021/cr030449l · Cited by 356
How can biochemical reactions within cells differ from those in test tubes?
Minton, A. P. (2015) · Journal of Cell Science · doi:10.1242/jcs.170183 · Cited by 320
Nonadditive effects of mixed crowding on protein stability
Batra, J., Xu, K., & Zhou, H. (2009) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.22425 · Cited by 109
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Metadata
- Authors
- Zhou, H.
- Venue
- Journal of Molecular Recognition
- Publisher
- Wiley
- Published
- 2004-08-31
- Volume
- 17
- Issue
- 5
- Pages
- 368-375
- ISSN
- 0952-3499 (ISSN-L)
- 1099-1352
- OpenAlex
- W2089625041
- Cited by
- 192
- References
- 6
- FWCI
- 3.72
- Type
- journal article
- Language
- en
- Open access
- bronze
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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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