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PubMed · 6863273

Free energy changes in lysozyme denaturation.

F Ahmad·C C Contaxis·C C Bigelow
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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.

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AnimalsChickensEgg WhiteGuanidineGuanidinesHot TemperatureKineticsMathematicsMuramidaseProtein ConformationProtein DenaturationThermodynamicsJournal ArticleResearch Support, Non-U.S. Gov't

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F Ahmad, C C Contaxis, C C Bigelow. 1983-07-10. Free energy changes in lysozyme denaturation.. https://pubmed.ncbi.nlm.nih.gov/6863273/

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