Combined pressure and temperature denaturation of ribonuclease A produces alternate denatured states

Protein folding, unfolding and misfolding have become critically important to a range of health and industry applications. Increasing high temperature and high pressure are used to control and speed up reactions. A number of studies have indicated that these parameters can have a large effect on protein structure and function. Here we describe the additive effects of these parameters on the small angle scattering behaviour of ribonuclease A. We find that alternate unfolded structures can be obtained with combined high pressure and temperature treatment of the protein. © 2016 Elsevier Inc.

Keywords

Protein denaturation, RNA-ASE, Small angle scattering, Neutron diffraction, Proteins, Protein structure

Citation

Ryan, T. M., Xun, Y., Cowieson, N. P., Mata, J. P., Jackson, A., Pauw, B. R., Smith, A. J., Kirby, N., & McGillivray, D. (2016). Combined pressure and temperature denaturation of ribonuclease A produces alternate denatured states. Biochemical and Biophysical Research Communications, 473(4), 834-839. doi:10.1016/j.bbrc.2016.03.135