標題: Intrinsic coordination for revealing local structural changes in protein folding-unfolding
作者: Shiu, Ying-Jen
Hayashi, Michitoshi
Shih, Orion
Su, Charlene
Tsai, Min-Yeh
Yeh, Yi-Qi
Su, Chun-Jen
Huang, Yu-Shan
Lin, Sheng-Hsien
Jeng, U-Ser
應用化學系
Department of Applied Chemistry
公開日期: 28-Jan-2016
摘要: With a deformed object of a rigid rod inside, the local dislocations may be tracked relatively easily with respect to the internal rigid rod. We apply this concept on protein folding-unfolding to track the internal structural changes of an unfolded protein in solution. Proposed here is a protein internal coordination based on the major axis X of an ellipsoidal protein and the stable intrinsic transition dipole moment mu of the protein during unfolding. In this methodology, small-angle X-ray scattering (SAXS) is used to provide the protein global morphologies in the native and unfolded states. Furthermore, time-resolved fluorescence anisotropy (TRFA) provides the relative orientation between X and mu of Trp59 of the model protein cytochrome c. Hence observed in the protein unfolding with denaturants, acid, urea, or GuHCl, is the elongation of the native protein conformation along a reoriented protein major axis; accompanied are the different extents of relocations of the terminal a helices and loop structures of the protein in the corresponding unfolding.
URI: http://dx.doi.org/10.1039/c5cp06309d
http://hdl.handle.net/11536/133030
ISSN: 1463-9076
DOI: 10.1039/c5cp06309d
期刊: PHYSICAL CHEMISTRY CHEMICAL PHYSICS
Volume: 18
Issue: 4
起始頁: 3179
結束頁: 3187
Appears in Collections:Articles