Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/24223
Title: Structural and dynamic changes of photoactive yellow protein during its photocycle in solution.
Authors: Rubinstenn, G
Vuister, GW
Mulder, FA
Düx, PE
Boelens, R
Hellingwerf, KJ
Kaptein, R
First Published: Jul-1998
Citation: NAT STRUCT BIOL, 1998, 5 (7), pp. 568-570
Abstract: 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 beta-sheet and parts of the helical structure are formed first and the region around the chromophore at a later stage.
DOI Link: 10.1038/823
ISSN: 1072-8368
Links: http://hdl.handle.net/2381/24223
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Biochemistry

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