The structure, stability, and folding process of amyloidogenic mutant human lysozyme.
The structure, stability, and folding process of amyloidogenic mutant human lysozyme.
复制标题
淀粉样蛋白突变体人溶菌酶的结构、稳定性和折叠过程。
DOI：
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发表时间：
1996
期刊：
影响因子：
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通讯作者：
K. Yutani
中科院分区：
文献类型：
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作者：
J. Funahashi;K. Takano;K. Ogasahara;Y. Yamagata;K. Yutani
为了阐明淀粉样蛋白形成的机制，对淀粉样变突变型人溶菌酶 (Ile56Thr) 的理化特性进行了检查。突变蛋白的晶体结构与野生型结构相同，只是引入的Thr56的羟基与蛋白内部的水分子形成了氢键。天然状态下突变蛋白的其他理化性质与野生型蛋白没有不同。然而，由于分子内部引入了极性残基（Thr），突变蛋白的平衡和动力学稳定性显着降低。可以得出结论，突变型人溶菌酶的淀粉样蛋白形成是由于倾向于（部分或/和完全）变性结构的倾向。
The physicochemical properties of an amyloidogenic mutant human lysozyme (Ile56Thr) were examined in order to elucidate the mechanism of amyloid formation. The crystal structure of the mutant protein was the same as the wild-type structure, except that the hydroxyl group of the introduced Thr56 formed a hydrogen bond with a water molecule in the interior of the protein. The other physicochemical properties of the mutant protein in the native state were not different from those of the wild-type protein. However, the equilibrium and kinetic stabilities of the mutant protein were remarkably decreased due to the introduction of a polar residue (Thr) in the interior of the molecule. It can be concluded that the amyloid formation of the mutant human lysozyme is due to a tendency to favor (partly or/and completely) denatured structures.