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• W1976553611 abstract "We refine a protein model that reproduces fundamental aspects of protein thermodynamics. The model exhibits two transitions, hot and cold unfolding. The number of relevant parameters is reduced to three: (1) binding energy of folding relative to the orientational energy of bound water, (2) ratio of degrees of freedom between the folded and unfolded protein chain, and (3) the number of water molecules that can access the hydrophobic parts of the protein interior upon unfolding. By increasing the number of water molecules in the model, the separation between the two peaks in the heat capacity curve comes closer, which is more consistent with experimental data. In the end we show that if we, as a speculative assumption, assign only two distinct energy levels for the bound water molecules, better correspondence with experiments can be obtained." @default.
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• W1976553611 date "2001-06-01" @default.
• W1976553611 modified "2023-10-17" @default.
• W1976553611 title "Thermodynamical Implications of a Protein Model with Water Interactions" @default.
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• W1976553611 doi "https://doi.org/10.1006/jtbi.2001.2311" @default.
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