Advances in high pressure bioscience and biotechnology ii, proceedings pages:69-72
International Conference on High Pressure Bioscience and Biotechnology edition:2 location:Dortmund, Germany date:16-19 September 2002
The pressure stability of ribonuclease A under native and reducing conditions was investigated with Fourier transform infrared spectroscopy. We observe that the pressure unfolded states in both cases are identical. However, upon decompression an amorphous aggregate is formed under the reducing conditions. In contrast, under native conditions ribonuclease A displays its classical reversible behavior. This difference is rationalized by assuming a higher degree of conformational fluctuations in the reduced unfolded state.