Version 1
: Received: 30 July 2024 / Approved: 31 July 2024 / Online: 1 August 2024 (05:03:37 CEST)
How to cite:
Izzi, G.; Campanile, M.; Del Vecchio, P.; Graziano, G. On the Stabilizing Effect of Aspartate and Glutamate and Its Counteraction by Common Denaturants. Preprints2024, 2024072532. https://doi.org/10.20944/preprints202407.2532.v1
Izzi, G.; Campanile, M.; Del Vecchio, P.; Graziano, G. On the Stabilizing Effect of Aspartate and Glutamate and Its Counteraction by Common Denaturants. Preprints 2024, 2024072532. https://doi.org/10.20944/preprints202407.2532.v1
Izzi, G.; Campanile, M.; Del Vecchio, P.; Graziano, G. On the Stabilizing Effect of Aspartate and Glutamate and Its Counteraction by Common Denaturants. Preprints2024, 2024072532. https://doi.org/10.20944/preprints202407.2532.v1
APA Style
Izzi, G., Campanile, M., Del Vecchio, P., & Graziano, G. (2024). On the Stabilizing Effect of Aspartate and Glutamate and Its Counteraction by Common Denaturants. Preprints. https://doi.org/10.20944/preprints202407.2532.v1
Chicago/Turabian Style
Izzi, G., Pompea Del Vecchio and Giuseppe Graziano. 2024 "On the Stabilizing Effect of Aspartate and Glutamate and Its Counteraction by Common Denaturants" Preprints. https://doi.org/10.20944/preprints202407.2532.v1
Abstract
By performing DSC measurements on RNase A, we studied the stabilization provided by the addition of potassium aspartate or potassium glutamate, that leads to a significant increase in the denaturation temperature of the protein. The stabilization proves to be mainly entropic in origin. A counteraction of the stabilization provided by KAsp or KGlu is obtained by adding common denaturants such as urea, guanidinium chloride and guanidinium thiocyanate. A rationalization of experimental data is devised on the basis of a theoretical approach developed by one of us. The main contribution to the conformational stability of globular proteins comes from the gain in translational entropy of water and co-solute ions and/or molecules for the decrease in solvent-excluded volume associated with polypeptide folding (i.e., there is a large decrease in solvent-accessible surface area). The magnitude of this entropic contribution increases with the number density and volume packing density of the solution. The two destabilizing contributions come from the conformational entropy of the chain, that should not depend significantly on the presence of co-solutes, and from the direct energetic interactions between co-solutes and the protein surface in both the native and denatured states. It is the magnitude of the latter to discriminate between stabilizing and destabilizing agents.
Keywords
aspartate; glutamate; protein conformational stability; denaturants; counteraction
Subject
Biology and Life Sciences, Biophysics
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
