Modeling hydration water and its role in polymer folding.
The hydrophobic effect is the dominant force which drives a proteintowards its native state, but its physics has not been thoroughlyunderstood yet. We introduce an exactly solvable model of the solvation ofnon-polar molecules in water, which shows that the reduced number ofallowed configurations of water molecules when the solute is present isenough to give rise to hydrophobic behaviour. We apply our model to anon-polar homopolymer in aqueous solution, obtaining a clear evidence ofboth `cold' and `warm' collapse transitions that recall those of proteins.Finally we show how the model can be adapted to describe the solvation ofaromatic and polar molecules.
Istituto Nazionale per la Fisica della Materia (INFM) and Dipartimento di Fisica, Politecnico di Torino, Corso Duca degli Abruzzi 24, I-10129 Torino, Italy.
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Bruscolini
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Casetti
Water; cold unfolding; hydrophobicity; polymer collapse; protein folding; statistical-mechanical models