Exploring fine structures of photoactive yellow protein in solution using wide-angle X-ray scattering

Tae Kyu Kim, Xiaobing Zuo, David M. Tiede, Hyotcherl Ihee

Research output: Contribution to journalArticle

3 Citations (Scopus)

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 A°-1 to 2.8 A°-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.

Original languageEnglish
Pages (from-to)1676-1680
Number of pages5
JournalBulletin of the Korean Chemical Society
Volume25
Issue number11
DOIs
Publication statusPublished - 2004 Nov 20

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X ray scattering
Proteins
Synchrotrons
Scattering
Fluxes
X rays
Experiments

All Science Journal Classification (ASJC) codes

  • Chemistry(all)

Cite this

Kim, Tae Kyu ; Zuo, Xiaobing ; Tiede, David M. ; Ihee, Hyotcherl. / Exploring fine structures of photoactive yellow protein in solution using wide-angle X-ray scattering. In: Bulletin of the Korean Chemical Society. 2004 ; Vol. 25, No. 11. pp. 1676-1680.
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Exploring fine structures of photoactive yellow protein in solution using wide-angle X-ray scattering. / Kim, Tae Kyu; Zuo, Xiaobing; Tiede, David M.; Ihee, Hyotcherl.

In: Bulletin of the Korean Chemical Society, Vol. 25, No. 11, 20.11.2004, p. 1676-1680.

Research output: Contribution to journalArticle

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