title: Free energy changes in lysozyme denaturation.
abstract: 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.
mesh_terms: D000818:Animals; D002645:Chickens; D004529:Egg White; D019791:Guanidine; D006146:Guanidines; D006358:Hot Temperature; D007700:Kinetics; D008433:Mathematics; D009113:Muramidase; D011487:Protein Conformation; D011489:Protein Denaturation; D013816:Thermodynamics
chemical_list: D006146:Guanidines; D009113:Muramidase; D019791:Guanidine