ArticleProceedings of the National Academy of Sciences of the United States of America2005
Phi values in protein-folding kinetics have energetic and structural components.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- A novel simplified structural design as an artificial enzyme for efficient hydrolysis of PNPA.Scientific reports · 2025Article
- Rate theories for biologists.Quarterly reviews of biophysics · 2010Review
- Analysis of oligomeric proteins during unfolding by pH and temperature.Journal of molecular modeling · 2009Article
- Probing the folding transition state structure of the villin headpiece subdomain via side chain and backbone mutagenesis.Journal of the American Chemical Society · 2009Article
- What have we learned from the studies of two-state folders, and what are the unanswered questions about two-state protein folding?Physical biology · 2009Article
- Identifying critical residues in protein folding: Insights from phi-value and P(fold) analysis.The Journal of chemical physics · 2008Article
- A two-state cell damage model under hyperthermic conditions: theory and in vitro experiments.Journal of biomechanical engineering · 2008Article
- Predicting protein folding rates from geometric contact and amino acid sequence.Protein science : a publication of the Protein Society · 2008Article
- A minimum-reaction-flux solution to master-equation models of protein folding.The Journal of chemical physics · 2008Article
- Rerouting the folding pathway of the Notch ankyrin domain by reshaping the energy landscape.Journal of the American Chemical Society · 2008Article
- Transition states in protein folding kinetics: modeling phi-values of small beta-sheet proteins.Biophysical journal · 2008Article
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3 authors.
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Abstract
Phi values are experimental measures of how the kinetics of protein folding is changed by single-site mutations. Phi values measure energetic quantities, but they are often interpreted in terms of the structures of the transition-state ensemble. Here, we describe a simple analytical model of the folding kinetics in terms of the formation of protein substructures. The model shows that Phi values have both structural and energetic components. It also provides a natural and general interpretation of "nonclassical" Phi values (i.e., < 0 or > 1). The model reproduces the Phi values for 20 single-residue mutations in the alpha-helix of the protein CI2, including several nonclassical Phi values, in good agreement with experiments.
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