ヒトリゾチーム変異体の構造に見るタンパク質の折れたたみ

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概要

• 論文の詳細を見る

• The folding pathway of a protein molecule <I>in vivo</I> is related to the formation of disulfide bonds. However, little is known about the mechanism of the folding process, because it is quite difficult to identify an intermediate in the formation of disulfide bonds during protein folding <I>in vivo</I>. Here, the relationship between protein folding and disulfide bond formation is discussed based on the results of the structural analyses of mutant human lysozymes, designated as C77/95A and C77A-a, in which a disulfide bond between Cys77 and Cys95 was modified.

• 日本結晶学会の論文

著者

• 伊中 浩治

  東京工業大学資源化学研究所

関連論文

• ヒトリゾチーム変異体の構造に見るタンパク質の折れたたみ

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