The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Protein structure, stability and solubility in water and other solvents
Open accessAbstract
Proteins carry out the most difficult tasks in living cells. They do so by interacting specifically with other molecules. This requires that they fold to a unique, globular conformation that is only marginally more stable than the large ensemble of unfolded states. The folded state is stabilized mainly by the burial and tight packing of over 80% of the peptide groups and non–polar side chains. If life as we know it is to exist in a solvent other than water, the folded state must be stable and soluble in the new solvent. Our analysis suggests that proteins will be unstable in most polar solvents such as ethanol, extremely stable in non–polar solvents such as cyclohexane, and even more stable in a vacuum. Our solubility studies suggest that protein solubility will be markedly lower in polar solvents such as ethanol and that proteins will be essentially insoluble in non–polar solvents such as cyclohexane. For these and other reasons it seems unlikely that the life we know could exist in any solvent system other than water.
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Citations
Cites
Guerois, R., Nielsen, J. E., & Serrano, L. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00442-4 · Cited by 1,728
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
Self-citationPacking Is a Key Selection Factor in the Evolution of Protein Hydrophobic Cores
Chen, J., & Stites, W. E. (2001) · Biochemistry · doi:10.1021/bi011776v · Cited by 84
Cited by
Contribution of hydrogen bonds to protein stability
Pace, C. N., Fu, H., Lee Fryar, K., Landua, J., Trevino, S. R., Schell, D., Thurlkill, R. L., Imura, S., Scholtz, J. M., Gajiwala, K., et al. (2014) · Protein Science · doi:10.1002/pro.2449 · Cited by 599
Protein Ionizable Groups: pK Values and Their Contribution to Protein Stability and Solubility
Pace, C. N., Grimsley, G. R., & Scholtz, J. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.r800080200 · Cited by 461
Structure and Energetics of the Hydrogen-Bonded Backbone in Protein Folding
Bolen, D. W., & Rose, G. D. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.061306.131357 · Cited by 408
Lapthorn, C., Pullen, F., & Chowdhry, B. Z. (2013) · Mass Spectrometry Reviews · doi:10.1002/mas.21349 · Cited by 398
Baldwin, R. L. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.05.078 · Cited by 305
Metadata
- Authors
- Nick Pace, C., Treviño, S., Prabhakaran, E., & Martin Scholtz, J.
- Venue
- Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences
- Publisher
- The Royal Society
- Published
- 2004-08-29
- Volume
- 359
- Issue
- 1448
- Pages
- 1225-1235
- ISSN
- 0962-8436 (ISSN-L)
- 1471-2970
- OpenAlex
- W2157607146
- Cited by
- 393
- References
- 3
- FWCI
- 3.06
- Type
- journal article
- Language
- en
- Open access
- green
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- Nick Pace, C., Treviño, S., Prabhakaran, E., & Martin Scholtz, J. (2004). Protein structure, stability and solubility in water and other solvents. Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences. https://doi.org/10.1098/rstb.2004.1500
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