Rate Determining Factors in Protein Model Structures

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dc.creatorBruscolini, Pierpaolo
dc.creatorPelizzola, Alessandro
dc.creatorZamparo, Marco
dc.date2007-09-14
dc.date.accessioned2026-07-07T08:29:37Z
dc.date.available2026-07-07T08:29:37Z
dc.descriptionPrevious research has shown a strong correlation of protein folding rates to the native state geometry, yet a complete explanation for this dependence is still lacking. Here we study the rate-geometry relationship with a simple statistical physics model, and focus on two classes of model geometries, representing ideal parallel and antiparallel structures. We find that the logarithm of the rate shows an almost perfect linear correlation with the "absolute contact order", but the slope depends on the particular class considered. We discuss these findings in the light of experimental results.
dc.description4 pages, 2 figures
dc.identifierhttps://arxiv.org/abs/0709.2243
dc.identifierhttp://arxiv.org/abs/0709.2243
dc.identifierPhys. Rev. Lett. 99, 038103 (2007)
dc.identifierdoi:10.1103/PhysRevLett.99.038103
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/138002
dc.subjectBiomolecules
dc.subjectStatistical Mechanics
dc.titleRate Determining Factors in Protein Model Structures
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