The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Unexpected Effects of Macromolecular Crowding on Protein Stability
Abstract
Most theories about macromolecular crowding focus on two ideas: the macromolecular nature of the crowder and entropy. For proteins, the volume excluded by the crowder favors compact native states over expanded denatured states, enhancing protein stability by decreasing the entropy of unfolding. We tested these ideas with the widely used crowding agent Ficoll-70 and its monomer, sucrose. Contrary to expectations, Ficoll and sucrose have approximately the same stabilizing effect on chymotrypsin inhibitor 2. Furthermore, the stabilization is driven by enthalpy, not entropy. These results point to the need for carefully controlled studies and more sophisticated theories for understanding crowding effects.
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Citations
Cites
Excluded volume as a determinant of macromolecular structure and reactivity
Minton, A. P. (1981) · Biopolymers · doi:10.1002/bip.1981.360201006 · Cited by 589
Minton, A. P., & Wilf, J. (1981) · Biochemistry · doi:10.1021/bi00520a003 · Cited by 320
Cited by
Protein Stabilization by Macromolecular Crowding through Enthalpy Rather Than Entropy
Senske, M., Törk, L., Born, B., Havenith, M., Herrmann, C., & Ebbinghaus, S. (2014) · Journal of the American Chemical Society · doi:10.1021/ja503205y · Cited by 284
Nerger, B. A., Brun, P.-T., & Nelson, C. M. (2019) · Soft Matter · doi:10.1039/c8sm02605j · Cited by 111
Metadata
- Authors
- Benton, L. A., Smith, A. E., Young, G. B., & Pielak, G. J.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2012-11-27
- Volume
- 51
- Issue
- 49
- Pages
- 9773-9775
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W1988517764
- Cited by
- 227
- References
- 2
- FWCI
- 6.85
- Type
- journal article
- Language
- en
- Open access
- closed
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- Benton, L. A., Smith, A. E., Young, G. B., & Pielak, G. J. (2012). Unexpected Effects of Macromolecular Crowding on Protein Stability. Biochemistry. https://doi.org/10.1021/bi300909q
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