Phi-values in protein folding kinetics have energetic and structural components

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dc.creatorMerlo, Claudia
dc.creatorDill, Ken A.
dc.creatorWeikl, Thomas R.
dc.date2005-07-14
dc.date.accessioned2026-07-07T05:59:23Z
dc.date.available2026-07-07T05:59:23Z
dc.descriptionPhi-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.
dc.description15 pages, 3 figures, 1 table
dc.identifierhttps://arxiv.org/abs/q-bio/0507025
dc.identifierhttp://arxiv.org/abs/q-bio/0507025
dc.identifierPNAS 102, 10171 (2005)
dc.identifierdoi:10.1073/pnas.0504171102
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/88658
dc.subjectBiomolecules
dc.subjectSoft Condensed Matter
dc.titlePhi-values in protein folding kinetics have energetic and structural components
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