Spectroscopic Study on the Pressure-Induced Conformation Change of Protein in Aqueous Solution

Pressure has been used for investigating the unfolding of proteins and for revealing their folding pathways and intermediates, even aggregate states. Since pressure can stabilize partially unfolded states and molten globules of proteins, which plays an important role both in chemical and biological phenomena in the aqueous solution. Here, we review several spectral methods developed for the study of pressure-induced conformation changes of proteins in solution, focus on infrared spectroscopy, fluorescence spectroscopy, small-angle X-ray scattering and so on, which can offer conformational information of proteins in solution in detail. The developing trends in this field are discussed and the outlook of the research area is also provided.