熱測定
Online ISSN : 1884-1899
Print ISSN : 0386-2615
ISSN-L : 0386-2615
解説
DSC により明らかになった蛋白質の高温での可逆的オリゴマー形成
城所 俊一
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ジャーナル フリー

2019 年 46 巻 1 号 p. 17-21

詳細
抄録
While irreversible aggregation or amyloid formation of denatured proteins are well known and studied in detail, the reversible oligomerization (RO) states of some monomeric proteins at high temperature have been recently discovered by DSC analysis. In this article, the RO states of horse cytochrome c and envelope protein domain 3 from dengue 4 virus were reviewed, and the essential points for the DSC analysis for such self-association/dissociation process were briefly introduced. The significance of RO was discussed as a key process for the kinetics of aggregation and/or amyloid formation, and the importance of the concentration dependence check was suggested for DSC analysis even for monomeric proteins.
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© 2019 日本熱測定学会
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