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Structural and dynamic changes of photoactive yellow protein during its photocycle in solution

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  • G. Rubinstenn, Bijvoet Ctr. for Biomolec. Research, Netherlands
  • G. W. Vuister, Bijvoet Ctr. for Biomolec. Research, Netherlands
  • F. A A Mulder
  • P. E. Dux, Bijvoet Ctr. for Biomolec. Research, Unknown
  • R. Boelens, Bijvoet Ctr. for Biomolec. Research, Netherlands
  • K. J. Hellingwerf, University of Amsterdam, Netherlands
  • R. Kaptein, Bijvoet Ctr. for Biomolec. Research, Netherlands

Light irradiation of photoactive yellow protein (PYP) induces a photocycle, in which red-shifted (pR) and blue-shifted (pB) intermediates have been characterized. An NMR study of the long-lived pB intermediate now reveals that it exhibits a large degree of disorder and exists as a family of multiple conformers that exchange on a millisecond time scale. This shows that the behavior of PYP in solution is different from what has been observed in the crystalline state. Furthermore, differential refolding to ground state pG is observed, whereby the central β-sheet and parts of the helical structure as formed first and the region around the chromophore at a later stage.

Original languageEnglish
JournalNature Structural Biology
Volume5
Issue7
Pages (from-to)568-570
Number of pages3
ISSN1072-8368
DOIs
Publication statusPublished - 20 Jul 1998
Externally publishedYes

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