Free energy changes in lysozyme denaturation.

Autor: Ahmad, F, Contaxis, C C, Bigelow, C C
Zdroj: Journal of Biological Chemistry; July 1983, Vol. 258 Issue: 13 p7960-7963, 4p
Abstrakt: Previous work has shown that native lysozyme (N) is completely denatured by the addition of guanidinium chloride (conformation D) but that partially denatured conformations appear in other denaturants. Conformation I appears when LiClO4 is added to the protein, and conformation II is caused by heating. We have now determined the apparent free energy changes for the reversible processes between N and the three unfolded conformations and for the process between II and D. This allows us to estimate the apparent free energy changes for a process between any two of these four conformations.
Databáze: Supplemental Index