Limited tryptic hydrolysis of faba bean legumin: Conformational stability of legumin‐T

T. Henning, S. Dudek, K. Schwenke, A. N. Danilenko, E. E. Braudo
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Abstract

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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蚕豆豆粕蛋白有限的胰蛋白酶水解:豆粕蛋白- T的构象稳定性
通过研究在盐酸胍存在下的平衡展开,评价了豆素和豆素- t的构象稳定性。得到的折叠/展开反应的热力学参数(25°C时的构象稳定性ΔG buffer o,其对变性剂浓度m和半变性剂浓度[变性剂]1/2的依赖)证明,在这些条件下,修饰成豆科蛋白- t后,豆科蛋白的构象稳定性只发生了相当小的下降。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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