Towards an Understanding of the Temperature/ Pressure Configurational and Free-Energy Landscape of Biomolecules

High Pressure X-ray Studies of Lipid Membranes and Lipid Phase Transitions

“…Interestingly, the volume and entropy changes for lipid phase transitions tend to vary in the same way, and since they appear as a ratio in the Clapeyron equation, the pressure dependence of the transition temperature for many different phase changes is remarkably similar [1,2,70] with t / generally in the range 2-3…”

Influence of High Pressure on the Dimerization of ToxR, a Protein Involved in Bacterial Signal Transduction

“…The physical state of the membrane affects the structure and function of membrane proteins, while in turn, integrated proteins can influence the phase state and lateral organization of the membrane. Until now, experiments on the influence of pressure on proteins and lipids have essentially been performed using monomeric and oligomeric proteins in aqueous solution and pure lipid bilayer systems, respectively (1,4,19). Still, little is known about the behavior upon pressurization of membrane proteins integrated in their natural lipid bilayer environment, and their putative function in pressure sensing and any in vivo data are missing.…”

Islet amyloid polypeptide and high hydrostatic pressure: towards an understanding of the fibrillization process

“…High hydrostatic pressure (HHP) has been widely used as a tool to understanding protein folding [16][17][18][19][20][21][22]. High pressure tends to destabilize proteins due the fact that the protein-solvent system in the unfolded state occupies a small volume than the system in the native state.…”

“…These effects seem to be caused by a combination of factors. The presence of cavities within the folded proteins or in the interface of oligomers favour unfolding or dissociation of these structures [16,17]. The dissociation of electrostatic interactions also leads to a marked reduction in the overall volume caused by electrostrictive effects of the water molecules around the unpaired charged residues [23].…”

“…The use of the pressure in studies of protein folding and stability can offer a great number of advantages [16,17]. Pressure affects only the volume of the system in focus, while the temperature denaturation, for example, involves changes in both volume and thermal energy of the system.…”