Modeling hydration water and its role in polymer folding

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dc.creatorBruscolini, Pierpaolo
dc.creatorCasetti, Lapo
dc.date2002-01-15
dc.date.accessioned2026-07-07T02:44:08Z
dc.date.available2026-07-07T02:44:08Z
dc.descriptionThe hydrophobic effect is the dominant force which drives a protein towards its native state, but its physics has not been thoroughly understood yet. We introduce an exactly solvable model of the solvation of non-polar molecules in water, which shows that the reduced number of allowed configurations of water molecules when the solute is present is enough to give rise to hydrophobic behaviour. We apply our model to a non-polar homopolymer in aqueous solution, obtaining a clear evidence of both ``cold'' and ``warm'' collapse transitions that recall those of proteins. Finally we show how the model can be adapted to describe the solvation of aromatic and polar molecules.
dc.description16 pages, 7 figures, LaTeX2e, needs kluwer.cls (included)
dc.identifierhttps://arxiv.org/abs/cond-mat/0201255
dc.identifierhttp://arxiv.org/abs/cond-mat/0201255
dc.identifierJournal of Biological Physics 27, 243 (2001)
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/18790
dc.subjectStatistical Mechanics
dc.subjectSoft Condensed Matter
dc.titleModeling hydration water and its role in polymer folding
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