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Stability Check of Succinylated Concanavalin A: Presence of Functionally Active Conformational State

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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.





Keywords: Molten Globule like state; Succinylated Con A; equilibrium denaturation; guanidine hydrochloride; urea

Document Type: Research Article

DOI: https://doi.org/10.2174/092986609787848117

Publication date: 2009-04-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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