ArticleBiomolecules2020
How Quickly Do Proteins Fold and Unfold, and What Structural Parameters Correlate with These Values?
Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Evolution of N-terminal mechanical lability as a determinant for Type III secretion.Protein science : a publication of the Protein Society · 2026Article
- High-pH NMR to Identify Macromolecular Hydrogen-Bonds and Foldons.Journal of the American Chemical Society · 2026Article
- Toward a systems metabolic engineering approach to improve thermotolerance of Escherichia coli.Microbial cell factories · 2026Review
- High-pH NMR to Identify Macromolecular Hydrogen-Bonds and Foldons.bioRxiv : the preprint server for biology · 2026Article
- A Type III secretion system effector evolved to be mechanically labile and initiate unfolding from the N-terminus.bioRxiv : the preprint server for biology · 2026Article
- Structure and stability of an apo thermophilic esterase that hydrolyzes polyhydroxybutyrate.Acta crystallographica. Section D, Structural biology · 2024Article
- Bioinformatics in Russia: history and present-day landscape.Briefings in bioinformatics · 2024Review
- Article
- Protein folding rate evolution upon mutations.Biophysical reviews · 2023Review
- An Inferred Ancestral CotA Laccase with Improved Expression and Kinetic Efficiency.International journal of molecular sciences · 2023Article
- Article
- Evolution of Protein Structure and Stability in Global Warming.International journal of molecular sciences · 2020Review
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Authors and funding
2 authors.
Funding
Abstract
The correlations between the logarithm of the unfolding rate of 108 proteins and their structural parameters were calculated. We showed that there is a good correlation between the logarithm of folding and unfolding rates (0.79) and protein stability and unfolding rate (0.79). Thus, the faster the protein folds, the faster it unfolds. Folding and unfolding rates are higher for the proteins with two-state kinetics, in comparison with the proteins with multi-state kinetics. At the same time, two-state bacterial proteins folds and unfolds two orders of magnitude faster than two-state eukaryotic proteins, and multi-state bacterial proteins folds and unfolds slower than multi-state eukaryotic proteins. Despite the fact that the folding rates of thermophilic and mesophilic proteins are close, the unfolding rates of thermophilic proteins is about two orders of magnitude lower than for mesophilic proteins. The correlation between unfolding rate and stability of thermophilic proteins is high (0.90). We also found that the unfolding rate correlates with such structural parameters as: size of the protein, radius of the cross-section, logarithm of absolute contact order, and radius of gyration. This information will be useful for engineering and designing new proteins with desired properties.
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