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

Sadaf      Fatima; Rizwan   Hasan   Khan

doi:10.2174/092986609787848117

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

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Protein & Peptide Letters

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

Volume: 16 Issue: 4

Author(s): Sadaf Fatima and Rizwan Hasan Khan

Affiliation:

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

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.

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Fatima Sadaf and Khan Hasan Rizwan, Stability Check of Succinylated Concanavalin A: Presence of Functionally Active Conformational State, Protein & Peptide Letters 2009; 16 (4) . https://dx.doi.org/10.2174/092986609787848117