The DOI matches its Crossref record; 89 of the 89 references it cites were found in a registry or an index.
Forces stabilizing proteins
Open accessAbstract
The goal of this article is to summarize what has been learned about the major forces stabilizing proteins since the late 1980s when site‐directed mutagenesis became possible. The following conclusions are derived from experimental studies of hydrophobic and hydrogen bonding variants. (1) Based on studies of 138 hydrophobic interaction variants in 11 proteins, burying a –CH 2− group on folding contributes 1.1 ± 0.5 kcal/mol to protein stability. (2) The burial of non‐polar side chains contributes to protein stability in two ways: first, a term that depends on the removal of the side chains from water and, more importantly, the enhanced London dispersion forces that result from the tight packing in the protein interior. (3) Based on studies of 151 hydrogen bonding variants in 15 proteins, forming a hydrogen bond on folding contributes 1.1 ± 0.8 kcal/mol to protein stability. (4) The contribution of hydrogen bonds to protein stability is strongly context dependent. (5) Hydrogen bonds by side chains and peptide groups make similar contributions to protein stability. (6) Polar group burial can make a favorable contribution to protein stability even if the polar group is not hydrogen bonded. (7) Hydrophobic interactions and hydrogen bonds both make large contributions to protein stability.
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Cites
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“In addition, global analyses based of the experimental results support this and show that hydrogen bonds make a favorable contribution to protein stability [93,94].”
BackgroundThe general theory of molecular forces
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Ligninolytic enzymes and its mechanisms for degradation of lignocellulosic waste in environment
Kumar, A., & Chandra, R. (2020) · Heliyon · doi:10.1016/j.heliyon.2020.e03170 · Cited by 648
Global analysis of protein folding using massively parallel design, synthesis, and testing
Rocklin, G. J., Chidyausiku, T. M., Goreshnik, I., Ford, A., Houliston, S., Lemak, A., Carter, L., Ravichandran, R., Mulligan, V. K., Chevalier, A., et al. (2017) · Science · doi:10.1126/science.aan0693 · Cited by 501
Meltome atlas—thermal proteome stability across the tree of life
Jarzab, A., Kurzawa, N., Hopf, T., Moerch, M., Zecha, J., Leijten, N., Bian, Y., Musiol, E., Maschberger, M., Stoehr, G., et al. (2020) · Nature Methods · doi:10.1038/s41592-020-0801-4 · Cited by 281
Collision induced unfolding of isolated proteins in the gas phase: past, present, and future
Dixit, S. M., Polasky, D. A., & Ruotolo, B. T. (2018) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2017.11.010 · Cited by 235
“One such element is protein stability, often reported as a free energy of protein unfolding and represents one of the most widely utilized descriptors of protein structure [3].”
BackgroundScarabelli, G., Oloo, E. O., Maier, J. K. X., & Rodriguez-Granillo, A. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167375 · Cited by 33
Metadata
- Authors
- Nick Pace, C., Scholtz, J. M., & Grimsley, G. R.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2014-05-17
- Volume
- 588
- Issue
- 14
- Pages
- 2177-2184
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2045529907
- Cited by
- 386
- References
- 89
- FWCI
- 7.54
- Type
- journal article
- Language
- en
- Open access
- green
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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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