Chapter 2 - Effects of high pressure on protein stability, structure, and function—Theory and applications

Abstract

Pressure is a powerful tool used to study basic protein science, modulate protein structure-function relationships for industrial applications, and gain insight into life in extreme environments. Despite its discovery over 100years ago, the physical basis governing pressure-induced unfolding remains controversial, although a reduction in total volume by protein conformational changes and/or solvent interactions are typically attributed to the phenomenon. However, nonvolume effects have also been considered. Recent advances in experimental techniques have made possible the study of folding energy landscapes reshaped under pressure. In addition to unfolding, under certain conditions, pressure may stabilize the native structure, folding intermediates, or aggregate structures. This chapter summarizes current knowledge on the mechanisms of protein structure and stability modulation under pressure and discusses how these effects can be leveraged for a variety of applications such as improving industrial catalysis, reducing food allergenicity, improving protein purification, and controlling protein aggregation.