Summary
Protein denaturation cooperativity varies depending on whether it is thermally, chemically, or pressure induced (1). Thermally induced unfolding showed the greatest cooperativity, followed by pressure then chemical (via guanidinium hydrochloride). However, pressure-based denaturation reduced protein volume, whereas thermal and chemical denaturation increased it. This was determined using apolipoprotein as a test case.
1.
Seelig J, Seelig A. Pressure Protein Denaturation Compared to Thermal and Chemical Unfolding: Analyses with Cooperative Models. The Journal of Physical Chemistry B. 2025;129(4):1229–36. Available from: https://doi.org/10.1021/acs.jpcb.4c07703