T. Henning, S. Dudek, K. Schwenke, A. N. Danilenko, E. E. Braudo
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Limited tryptic hydrolysis of faba bean legumin: Conformational stability of legumin‐T
The conformational stability of legumin and legumin-T was evaluated by studying the equilibrium unfolding in the presence of guanidine hydrochloride. The obtained thermodynamic parameters for the folding/unfolding-reaction (conformational stability ΔG buffer o at 25 °C, its dependence on denaturant concentration m and the half denaturant concentration value [denaturant] 1/2 ) provided evidence that only a rather small decrease in the conformational stability of the legumin after modification to legumin-T occurs under these conditions.
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