Stability check of succinylated concanavalin A: presence of functionally active conformational state.
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.
Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh - 202002, India.
Sadaf
S
Fatima
Rizwan Hasan
RH
Khan
D003208:Concanavalin A / Q000737:chemistry*; D019791:Guanidine / Q000494:pharmacology; D006358:Hot Temperature; D011487:Protein Conformation / Q000187:drug effects*; D011489:Protein Denaturation; D017510:Protein Folding / Q000187:drug effects; D055503:Protein Multimerization; D055550:Protein Stability; D013050:Spectrometry, Fluorescence; D014508:Urea / Q000494:pharmacology
D003208:Concanavalin A; C019558:succinylconcanavalin A; D014508:Urea; D019791:Guanidine