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

研究成果: 雜誌貢獻文章

4 引文 (Scopus)

摘要

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.
原文英語
頁(從 - 到)2171-2178
頁數8
期刊Journal of Thermal Analysis and Calorimetry
115
發行號3
DOIs
出版狀態已發佈 - 三月 2014

指紋

Securin
folding
Thermodynamic stability
thermal stability
proteins
Intrinsically Disordered Proteins
Kinetics
kinetics
Proteins
Glass transition
glass
titration
heat measurement
Fluorescence spectroscopy
Calorimetry
Titration
Particle size analysis
fluorescence
Conformations
scanning

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Condensed Matter Physics

引用此文

Thermal stability and folding kinetics analysis of disordered protein, securin. / Chu, Hsueh Liang; Chen, Tzu Hsuan; Wu, Chang You; Yang, Yao Chen; Tseng, Shin Hua; Cheng, Tsai Mu; Ho, Li Ping; Tsai, Li Yun; Li, Hsing Yuan; Chang, Chia Seng; Chang, Chia Ching.

於: Journal of Thermal Analysis and Calorimetry, 卷 115, 編號 3, 03.2014, p. 2171-2178.

研究成果: 雜誌貢獻文章

Chu, HL, Chen, TH, Wu, CY, Yang, YC, Tseng, SH, Cheng, TM, Ho, LP, Tsai, LY, Li, HY, Chang, CS & Chang, CC 2014, 'Thermal stability and folding kinetics analysis of disordered protein, securin', Journal of Thermal Analysis and Calorimetry, 卷 115, 編號 3, 頁 2171-2178. https://doi.org/10.1007/s10973-013-3598-x
Chu, Hsueh Liang ; Chen, Tzu Hsuan ; Wu, Chang You ; Yang, Yao Chen ; Tseng, Shin Hua ; Cheng, Tsai Mu ; Ho, Li Ping ; Tsai, Li Yun ; Li, Hsing Yuan ; Chang, Chia Seng ; Chang, Chia Ching. / Thermal stability and folding kinetics analysis of disordered protein, securin. 於: Journal of Thermal Analysis and Calorimetry. 2014 ; 卷 115, 編號 3. 頁 2171-2178.
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abstract = "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.",
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AU - Chu, Hsueh Liang

AU - Chen, Tzu Hsuan

AU - Wu, Chang You

AU - Yang, Yao Chen

AU - Tseng, Shin Hua

AU - Cheng, Tsai Mu

AU - Ho, Li Ping

AU - Tsai, Li Yun

AU - Li, Hsing Yuan

AU - Chang, Chia Seng

AU - Chang, Chia Ching

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N2 - 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.

AB - 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.

KW - Disordered protein

KW - Folding kinetics

KW - Securin

KW - Thermal stability

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