Netsu Sokutei
Online ISSN : 1884-1899
Print ISSN : 0386-2615
ISSN-L : 0386-2615
Review
Reversible Oligomerization of Proteins at High Temperature Revealed by DSC Analysis
Shun-ichi Kidokoro
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JOURNAL FREE ACCESS

2019 Volume 46 Issue 1 Pages 17-21

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Abstract
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 The Japan Society of Calorimetry and Thermal Analysis
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