The DOI matches its Crossref record; 51 of the 51 references it cites were found in a registry or an index.
Macromolecular Crowding and Protein Stability
Abstract
An understanding of cellular chemistry requires knowledge of how crowded environments affect proteins. The influence of crowding on protein stability arises from two phenomena, hard-core repulsions and soft (i.e., chemical) interactions. Most efforts to understand crowding effects on protein stability, however, focus on hard-core repulsions, which are inherently entropic and stabilizing. We assessed these phenomena by measuring the temperature dependence of NMR-detected amide proton exchange and used these data to extract the entropic and enthalpic contributions of crowding to the stability of ubiquitin. Contrary to expectations, the contribution of chemical interactions is large and in many cases dominates the contribution from hardcore repulsions. Our results show that both chemical interactions and hard-core repulsions must be considered when assessing the effects of crowding and help explain previous observations about protein stability and dynamics in cells.
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Cites
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Physicochemical Properties of Cells and Their Effects on Intrinsically Disordered Proteins (IDPs)
Theillet, F.-X., Binolfi, A., Frembgen-Kesner, T., Hingorani, K., Sarkar, M., Kyne, C., Li, C., Crowley, P. B., Gierasch, L., Pielak, G. J., et al. (2014) · Chemical Reviews · doi:10.1021/cr400695p · Cited by 503
Self-citationTardigrades Use Intrinsically Disordered Proteins to Survive Desiccation
Boothby, T. C., Tapia, H., Brozena, A. H., Piszkiewicz, S., Smith, A. E., Giovannini, I., Rebecchi, L., Pielak, G. J., Koshland, D., & Goldstein, B. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.02.018 · Cited by 409
Self-citationProtein 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
Soft interactions and crowding
Sarkar, M., Li, C., & Pielak, G. J. (2013) · Biophysical Reviews · doi:10.1007/s12551-013-0104-4 · Cited by 276
Self-citationIslet amyloid polypeptide: structure, function, and pathophysiology
Akter, R., Cao, P., Noor, H., Ridgway, Z., Tu, L.-H., Wang, H., Wong, A. G., Zhang, X., Abedini, A., Schmidt, A. M., et al. (2016) · Journal of Diabetes Research · doi:10.1155/2016/2798269 · Cited by 273
(2023) · doi:10.1038/s41467-023-41586-y · Cited by 118
Molecular Crowding and Early Evolution
Saha, R., Pohorille, A., & Chen, I. A. (2014) · Origins of Life and Evolution of Biospheres · doi:10.1007/s11084-014-9392-3 · Cited by 52
Molecular crowding favors reactivity of a human ribozyme under physiological ionic conditions
Strulson, C. A., Yennawar, N. H., Rambo, R. P., & Bevilacqua, P. C. (2013) · Biochemistry · doi:10.1021/bi400816s · Cited by 46
Metadata
- Authors
- Wang, Y., Sarkar, M., Smith, A. E., Krois, A. S., & Pielak, G. J.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2012-09-27
- Volume
- 134
- Issue
- 40
- Pages
- 16614-16618
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2323551623
- Cited by
- 346
- References
- 51
- FWCI
- 11.15
- Type
- journal article
- Language
- en
- Open access
- closed
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