dorsal/arxiv
View SchemaPhi-values in protein folding kinetics have energetic and structural components
| Authors | Claudia Merlo, Ken A. Dill, Thomas R. Weikl |
|---|---|
| Categories | |
| ArXiv ID | q-bio/0507025 |
| URL | https://arxiv.org/abs/q-bio/0507025 |
| DOI | 10.1073/pnas.0504171102 |
| Journal | PNAS 102, 10171 (2005) |
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 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. In addition, it provides a natural and general interpretation of "nonclassical" Phi-values (i.e., less than zero, or greater than one). 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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"abstract": "Phi-values are experimental measures of how the kinetics of protein folding\nis changed by single-site mutations. Phi-values measure energetic quantities,\nbut are often interpreted in terms of the structures of the transition state\nensemble. Here we describe a simple analytical model of the folding kinetics in\nterms of the formation of protein substructures. The model shows that\nPhi-values have both structural and energetic components. In addition, it\nprovides a natural and general interpretation of \"nonclassical\" Phi-values\n(i.e., less than zero, or greater than one). The model reproduces the\nPhi-values for 20 single-residue mutations in the alpha-helix of the protein\nCI2, including several nonclassical Phi-values, in good agreement with\nexperiments.",
"arxiv_id": "q-bio/0507025",
"authors": [
"Claudia Merlo",
"Ken A. Dill",
"Thomas R. Weikl"
],
"categories": [
"q-bio.BM",
"cond-mat.soft"
],
"doi": "10.1073/pnas.0504171102",
"journal_ref": "PNAS 102, 10171 (2005)",
"title": "Phi-values in protein folding kinetics have energetic and structural components",
"url": "https://arxiv.org/abs/q-bio/0507025"
},
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