Contribution of Water to Pressure and Cold Denaturation of Proteins

Abstract

The mechanisms of cold- and pressure-denaturation of proteins are matter of debate and are commonly understood as due to water-mediated interactions. Here we study several cases of proteins, with or without a unique native state, with or without hydrophilic residues, by means of a coarse-grain protein model in explicit solvent. We show, using Monte Carlo simulations, that taking into account how water at the protein interface changes its hydrogen bond properties and its density fluctuations is enough to predict protein stability regions with elliptic shapes in the temperature-pressure plane, consistent with previous theories. Our results clearly identify the different mechanisms with which water participates to denaturation and open the perspective to develop advanced computational design tools for protein engineering.

arXiv comment6 pages, 4 figures

References in corpus (8)

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• Microscopic mechanism for cold denaturation
• Intra-molecular coupling as a mechanism for a liquid-liquid phase transition
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Cited by in corpus (9)

• Protein Unfolding and Aggregation near a Hydrophobic Interface
• Consistent treatment of hydrophobicity in protein lattice models accounts for cold denaturation
• In silico evidence that protein unfolding is as a precursor of the protein aggregation
• Hydrogen bond correlated percolation in a supercooled water monolayer as a hallmark of the critical region
• Using Car-Parrinello simulations and microscopic order descriptors to reveal two locally favored structures with distinct molecular dipole moments and dynamics in ambient liquid water
• Many-Body Contributions in Water Nano-Clusters
• A Tale of Two Desolvation Potentials: An Investigation of Protein Behavior Under High Hydrostatic Pressure
• Hydrophobic homopolymer's coil-globule transition and adsorption onto a hydrophobic surface under different conditions
• The structural order of protein hydration water