Revisiting volume changes in pressure-induced protein unfolding.
It has long been known that the application of hydrostatic pressure generally leads to the unfolding of proteins. Despite a relatively large number of reports in the literature over the past few decades, there has been great confusion over the sign and magnitude as well as the fundamental factors contributing to volume effects in protein conformational transitions. It is the goal of this review to present and discuss the results obtained concerning the sign and magnitude of the volume changes accompanying the unfolding of proteins. The vast majority of cases point to a significant decrease in volume upon unfolding. Nonetheless, there is evidence that, due to differences in the thermal expansivity of the folded and unfolded states of proteins reported in a half dozen manuscripts, that the sign of the volume change may become positive at higher temperatures.
Royer
Catherine A
CA
Centre de Biochimie Structurale, INSERM U554, CNRS UMR 5048, Montpellier, France. royer@cbs.cnrs.fr
D006874:Hydrostatic Pressure; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
D011506:Proteins