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还原型溶菌酶复性早期折叠成天然构象的肽段区域的鉴定。

Identification of the peptide region that folds native conformation in the early stage of the renaturation of reduced lysozyme.

作者信息

Ueda T, Ohkuri T, Imoto T

机构信息

Graduate School of Pharmaceutical Sciences, Kyushu University, Fukuoka, Japan.

出版信息

Biochem Biophys Res Commun. 1996 Nov 1;228(1):203-8. doi: 10.1006/bbrc.1996.1640.

Abstract

We prepared three peptide fragments (fg.59-105, fg.63-105 and fg.64-105) by the BrCN cleavage of mutant lysozymes where Ile58, Trp62 and Trp63 were mutated to Met, respectively. From the analysis of formation of the disulfide bonds among Cys64, Cys76, Cys80 and Cys94 in the renaturation of each peptide fragment from the reduced form, Trp62 and Trp63 were required for the effective formation of two disulfide bonds. Especially, Trp62 was found to be involved in the correct formation of the disulfide bonds.

摘要

我们通过对突变型溶菌酶进行溴化氰裂解制备了三个肽片段(图59 - 105、图63 - 105和图64 - 105),其中异亮氨酸58、色氨酸62和色氨酸63分别突变为甲硫氨酸。通过对每个还原形式的肽片段复性过程中半胱氨酸64、半胱氨酸76、半胱氨酸80和半胱氨酸94之间二硫键形成的分析,发现色氨酸62和色氨酸63对于两个二硫键的有效形成是必需的。特别是,发现色氨酸62参与了二硫键的正确形成。

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