Thermal stability and folding kinetics analysis of disordered protein, securin

Hsueh Liang Chu, Tzu Hsuan Chen, Chang You Wu, Yao Chen Yang, Shin Hua Tseng, Tsai Mu Cheng, Li Ping Ho, Li Yun Tsai, Hsing Yuan Li, Chia Seng Chang, Chia Ching Chang

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)


Lacking a stable tertiary structure, intrinsically disordered proteins (IDPs) possess particular functions in cell regulation, signaling, and controlling pathways. The study of their unique structural features, thermal stabilities, and folding kinetics is intriguing. In this study, an identified IDP, securin, was used as a model protein. By using a quasi-static five-step (on-path) folding process, the function of securin was restored and analyzed by isothermal titration calorimetry. Fluorescence spectroscopy and particle size analysis indicated that securin possessed a compact hydrophobic core and particle size. The glass transition of securin was characterized using differential scanning microcalorimetry. Furthermore, the folding/unfolding rates (kobs) of securin were undetectable, implying that the folding/unfolding rate is very fast and that the conformation of securin is sensitive to solvent environmental change. Therefore, securin may fold properly under specific physiological conditions. In summary, the thermal glass transition behavior and undetectable kobs of folding/unfolding reactions may be two of the indices of IDP.

Original languageEnglish
Pages (from-to)2171-2178
Number of pages8
JournalJournal of Thermal Analysis and Calorimetry
Issue number3
Publication statusPublished - Mar 2014


  • Disordered protein
  • Folding kinetics
  • Securin
  • Thermal stability

ASJC Scopus subject areas

  • Condensed Matter Physics
  • Materials Chemistry
  • Polymers and Plastics
  • General Dentistry
  • Physical and Theoretical Chemistry


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