Title: Pressure unfolded states of ribonuclease A under native and reducing conditions have identical conformations
Authors: Meersman, Filip
Heremans, Karel #
Issue Date: 2003
Publisher: Springer-verlag berlin
Host Document: Advances in high pressure bioscience and biotechnology ii, proceedings pages:69-72
Conference: International Conference on High Pressure Bioscience and Biotechnology edition:2 location:Dortmund, Germany date:16-19 September 2002
Abstract: 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.
Publication status: published
KU Leuven publication type: IC
Appears in Collections:Molecular Imaging and Photonics
Biochemistry, Molecular and Structural Biology Section
# (joint) last author

Files in This Item:

There are no files associated with this item.

Request a copy


All items in Lirias are protected by copyright, with all rights reserved.

© Web of science