ArticleProtein science : a publication of the Protein Society2009
Predicting repeat protein folding kinetics from an experimentally determined folding energy landscape.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Identification of an on-pathway intermediate illuminates the kinetic competition between protein folding and misfolding.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Discovery of an on-pathway protein folding intermediate illuminates the kinetic competition between folding and misfolding.bioRxiv : the preprint server for biology · 2024Article
- Large Ankyrin repeat proteins are formed with similar and energetically favorable units.PloS one · 2020Article
- Capturing coevolutionary signals inrepeat proteins.BMC bioinformatics · 2015Article
- Structure of a partially unfolded form of Escherichia coli dihydrofolate reductase provides insight into its folding pathway.Protein science : a publication of the Protein Society · 2014Article
- Frustration in biomolecules.Quarterly reviews of biophysics · 2014Review
- General mechanism of two-state protein folding kinetics.Journal of the American Chemical Society · 2014Article
- A disorder-induced domino-like destabilization mechanism governs the folding and functional dynamics of the repeat protein IκBα.PLoS computational biology · 2013Article
- Metastability of papain and the molecular mechanism for its sequential acid-denaturation.The protein journal · 2011Article
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Authors and funding
2 authors.
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Abstract
The Notch ankyrin domain is a repeat protein whose folding has been characterized through equilibrium and kinetic measurements. In previous work, equilibrium folding free energies of truncated constructs were used to generate an experimentally determined folding energy landscape (Mello and Barrick, Proc Natl Acad Sci USA 2004;101:14102-14107). Here, this folding energy landscape is used to parameterize a kinetic model in which local transition probabilities between partly folded states are based on energy values from the landscape. The landscape-based model correctly predicts highly diverse experimentally determined folding kinetics of the Notch ankyrin domain and sequence variants. These predictions include monophasic folding and biphasic unfolding, curvature in the unfolding limb of the chevron plot, population of a transient unfolding intermediate, relative folding rates of 19 variants spanning three orders of magnitude, and a change in the folding pathway that results from C-terminal stabilization. These findings indicate that the folding pathway(s) of the Notch ankyrin domain are thermodynamically selected: the primary determinants of kinetic behavior can be simply deduced from the local stability of individual repeats.
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