Abstract
The equilibrium denaturation pathway of Succinyl Con A exhibited three-state mechanism with the transition midpoints at 1 and 3 M GdnHCl and at 2.6 and 5 M urea. Unfolding resulted in stabilization of molten-globule (MG) like intermediate states at 2 M GdnHCl and 3 M urea. It was particularly interesting that state obtained at 3 M urea was functionally active.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Concanavalin A / chemistry*
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Guanidine / pharmacology
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Hot Temperature
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Protein Conformation / drug effects*
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Protein Denaturation
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Protein Folding / drug effects
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Protein Multimerization
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Protein Stability
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Spectrometry, Fluorescence
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Urea / pharmacology
Substances
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Concanavalin A
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succinylconcanavalin A
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Urea
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Guanidine