Thermodynamical implications of a protein model with water interactions

Details Thermodynamical implications of a protein model with water interactions Thermodynamical implications of a protein model with water interactions

2000-07-05

arxiv.org/abs/cond-mat/0007078v1

Physics

Condensed Matter

8 pages LaTeX, 6 Postscript figures

Scientific paper

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. By increasing the number of water molecules in the model, the separation between the two peaks in the heat capacity curve decreases, which is more consistent with experimental data. We also show that if we, as a speculative assumption, assign effectively only two distinct energy levels for the bound water molecules, the hot peak in the heat capacity curve will be larger than the cold peak, in accordance with experimental observations.

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