The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Stabilization of Proteins in Confined Spaces
Abstract
We present theory showing that confining a protein to a small inert space (a "cage") should stabilize the protein against reversible unfolding. Examples of such spaces might include the pores within chromatography columns, the Anfinsen cage in chaperonins, the interiors of ribosomes, or regions of steric occlusion inside cells. Confinement eliminates some expanded configurations of the unfolded chain, shifting the equilibrium from the unfolded state toward the native state. The partition coefficient for a protein in a confined space is predicted to decrease significantly when the solvent is changed from native to denaturing conditions. Small cages are predicted to increase the stability of the native state by as much as 15 kcal/mol. Confinement may also increase the rates of protein or RNA folding.
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Cited by
Molecular crowding enhances native state stability and refolding rates of globular proteins
Cheung, M. S., Klimov, D., & Thirumalai, D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409630102 · Cited by 558
Mesoporous materials for encapsulating enzymes
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Protein aggregation in crowded environments
Ellis, R. J., & Minton, A. P. (2006) · Biological Chemistry · doi:10.1515/bc.2006.064 · Cited by 421
The sol-gel encapsulation of enzymes
Pierre, A. C. (2004) · Biocatalysis and Biotransformation · doi:10.1080/10242420412331283314 · Cited by 384
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
Metadata
- Authors
- Zhou, H.-X., & Dill, K. A.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2001-08-29
- Volume
- 40
- Issue
- 38
- Pages
- 11289-11293
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2062110094
- Cited by
- 386
- References
- 10
- FWCI
- 4.34
- Type
- journal article
- Language
- en
- Open access
- closed
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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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