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http://dx.doi.org/10.5012/bkcs.2004.25.11.1676

Exploring Fine Structures of Photoactive Yellow Protein in Solution Using Wide-Angle X-ray Scattering  

Kim, Tae-Kyu (Department of Chemistry and School of Molecular Science (BK21), KAIST)
Zuo, Xiaobing (Chemistry Division, Argonne National Laboratory)
Tiede, David M. (Chemistry Division, Argonne National Laboratory)
Ihee, Hyot-Cherl (Department of Chemistry and School of Molecular Science (BK21), KAIST)
Publication Information
Bulletin of the Korean Chemical Society / v.25, no.11, 2004 , pp. 1676-1680 More about this Journal
Abstract
We demonstrate that wide-angle X-ray scattering pattern from photoactive yellow protein (PYP) in solution using a high flux third generation synchrotron X-ray source reflects not only the overall structure, but also fine structures of the protein. X-ray scattering data from PYP in solution have been collected in q ranges from 0.02 ${\AA}^{-1}$ to 2.8 ${\AA}^{-1}$. These data are sensitive to the protein structure and consistent with the calculation based on known crystallographic atomic coordinates. Theoretical scattering patterns were also calculated for the intermediates during the photocycle of PYP to estimate the feasibility of time-resolved wide-angle X-ray scattering experiments on such proteins. These results demonstrate the possibility of using the wide-angle solution X-ray scattering as a quantitative monitor of photo-induced structural changes in PYP.
Keywords
Wide-angle X-ray scattering; Photoactive yellow protein; Time-resolved; Biological macromolecule; 3-Dimensional structure;
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