Microscopic mechanism for cold denaturation
arXiv:0704.2787 · doi:10.1103/PhysRevLett.100.118101
Abstract
We elucidate the mechanism of cold denaturation through constant-pressure simulations for a model of hydrophobic molecules in an explicit solvent. We find that the temperature dependence of the hydrophobic effect is the driving force/induces/facilitates cold denaturation. The physical mechanism underlying this phenomenon is identified as the destabilization of hydrophobic contact in favor of solvent separated configurations, the same mechanism seen in pressure induced denaturation. A phenomenological explanation proposed for the mechanism is suggested as being responsible for cold denaturation in real proteins.
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Cited by in corpus (13)
- Contribution of Water to Pressure and Cold Denaturation of Proteins
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- Phase behavior of blocky charge lattice polymers: Crystals, liquids, sheets, filaments and clusters
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