title: On the effect of hydrostatic pressure on the conformational stability of globular proteins.
abstract: The model developed for cold denaturation (Graziano, PCCP 2010, 12, 14245-14252) is extended to rationalize the dependence of protein conformational stability upon hydrostatic pressure, at room temperature. A pressure- volume work is associated with the process of cavity creation for the need to enlarge the liquid volume against hydrostatic pressure. This contribution destabilizes the native state that has a molecular volume slightly larger than the denatured state due to voids existing in the protein core. Therefore, there is a hydrostatic pressure value at which the pressure-volume contribution plus the conformational entropy loss of the polypeptide chain are able to overwhelm the stabilizing gain in translational entropy of water molecules, due to the decrease in water accessible surface area upon folding, causing denaturation.
authors: Dipartimento di Scienze e Tecnologie, Università del Sannio, via Port'arsa 11, Benevento, 82100, Italy.
authors: Giuseppe
authors: G
authors: Graziano
mesh_terms: D006874:Hydrostatic Pressure; D011487:Protein Conformation; D055550:Protein Stability; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D013696:Temperature
chemical_list: D011506:Proteins
keywords: geometric model of proteins; pressure-induced denaturation; pressure−volume work; solvent-excluded volume effect; voids in the protein core