Cold and Warm Denaturation of Hydrophobic Polymers

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dc.creatorRios, Paolo De Los
dc.creatorCaldarelli, Guido
dc.date1999-03-26
dc.date1999-12-18
dc.date.accessioned2026-07-07T03:13:08Z
dc.date.available2026-07-07T03:13:08Z
dc.descriptionWe introduce a polymer model where the transition from swollen to compact configurations is due to interactions between the monomers and the solvent. These interactions are the origin of the effective attractive interactions between hydrophobic amminoacids in proteins. We find that in the low and high temperature phases polymers are swollen, and there is an intermediate phase where the most favorable configurations are compact. We argue that such a model captures in a single framework both the cold and the warm denaturation experimentally detected for proteins. Some consequences for protein folding are discussed.
dc.descriptionLateX, 4 .eps figures
dc.identifierhttps://arxiv.org/abs/cond-mat/9903394
dc.identifierhttp://arxiv.org/abs/cond-mat/9903394
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/29180
dc.subjectStatistical Mechanics
dc.subjectSoft Condensed Matter
dc.subjectQuantitative Biology
dc.titleCold and Warm Denaturation of Hydrophobic Polymers
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