Studying submicrosecond protein folding kinetics using a photolabile caging strategy and time-resolved photoacoustic calorimetry

Hsin Liang Chen, Jack C.C. Hsu, Man Hoang Viet, Mai Suan Li, Chin Kun Hu, Chia Hsun Liu, Frederick Y. Luh, Silvia S.W. Chen, Evan S.H. Chang, Andrew H.J. Wang, Min Feng Hsu, Wunshain Fann, Rita P.Y. Chen

研究成果: 雜誌貢獻文章同行評審

6 引文 斯高帕斯(Scopus)

摘要

Kinetic measurement of protein folding is limited by the method used to trigger folding. Traditional methods, such as stopped flow, have a long mixing dead time and cannot be used to monitor fast folding processes. Here, we report a compound, 4-(bromomethyl)-6,7-dimethoxycoumarin, that can be used as a "photolabile cage" to study the early stages of protein folding. The folding process of a protein, RD1, including kinetics, enthalpy, and volume change, was studied by the combined use of a phototriggered caging strategy and time-resolved photoacoustic calorimetry. The cage caused unfolding of the photolabile protein, and then a pulse UV laser (~10 -9 s) was used to break the cage, leaving the protein free to refold and allowing the resolving of two folding events on a nanosecond time scale. This strategy is especially good for monitoring fast folding proteins that cannot be studied by traditional methods.

原文英語
頁(從 - 到)2973-2983
頁數11
期刊Proteins: Structure, Function and Bioinformatics
78
發行號14
DOIs
出版狀態已發佈 - 11月 1 2010
對外發佈

ASJC Scopus subject areas

  • 結構生物學
  • 生物化學
  • 分子生物學

指紋

深入研究「Studying submicrosecond protein folding kinetics using a photolabile caging strategy and time-resolved photoacoustic calorimetry」主題。共同形成了獨特的指紋。

引用此