The response of c-terminal variants of ribonuclease a to pressure and temperature-induced unfolding. A study by fourth derivative UV and Fourier Transform Infrared spectroscopy

Abstract The effect of pressure and temperature on ribonuclease A WT and a set of variants was studied by fourth derivative UV and Fourier Transform Infrared spectroscopy. The results reveal an unusual similarity between pressure- and temperature-induced unfolding and indicate the importance of the region extending from residue 106 to 118 (of 124) in stability and probably in the early stages of folding.