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

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Structural and dynamic changes of photoactive yellow protein during its photocycle in solution. / Rubinstenn, G.; Vuister, G. W.; Mulder, F. A A et al.

In: Nature Structural Biology, Vol. 5, No. 7, 20.07.1998, p. 568-570.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Rubinstenn, G, Vuister, GW, Mulder, FAA, Dux, PE, Boelens, R, Hellingwerf, KJ & Kaptein, R 1998, 'Structural and dynamic changes of photoactive yellow protein during its photocycle in solution', Nature Structural Biology, vol. 5, no. 7, pp. 568-570. https://doi.org/10.1038/823

APA

Rubinstenn, G., Vuister, G. W., Mulder, F. A. A., Dux, P. E., Boelens, R., Hellingwerf, K. J., & Kaptein, R. (1998). Structural and dynamic changes of photoactive yellow protein during its photocycle in solution. Nature Structural Biology, 5(7), 568-570. https://doi.org/10.1038/823

CBE

Rubinstenn G, Vuister GW, Mulder FAA, Dux PE, Boelens R, Hellingwerf KJ, Kaptein R. 1998. Structural and dynamic changes of photoactive yellow protein during its photocycle in solution. Nature Structural Biology. 5(7):568-570. https://doi.org/10.1038/823

MLA

Vancouver

Rubinstenn G, Vuister GW, Mulder FAA, Dux PE, Boelens R, Hellingwerf KJ et al. Structural and dynamic changes of photoactive yellow protein during its photocycle in solution. Nature Structural Biology. 1998 Jul 20;5(7):568-570. https://doi.org/10.1038/823

Author

Rubinstenn, G. ; Vuister, G. W. ; Mulder, F. A A et al. / Structural and dynamic changes of photoactive yellow protein during its photocycle in solution. In: Nature Structural Biology. 1998 ; Vol. 5, No. 7. pp. 568-570.

Bibtex

@article{4b46f1eecf134f119d4b9de7d3de9d94,
title = "Structural and dynamic changes of photoactive yellow protein during its photocycle in solution",
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 β-sheet and parts of the helical structure as formed first and the region around the chromophore at a later stage.",
author = "G. Rubinstenn and Vuister, {G. W.} and Mulder, {F. A A} and Dux, {P. E.} and R. Boelens and Hellingwerf, {K. J.} and R. Kaptein",
year = "1998",
month = jul,
day = "20",
doi = "10.1038/823",
language = "English",
volume = "5",
pages = "568--570",
journal = "Nature Structural and Molecular Biology",
issn = "1545-9993",
publisher = "Nature Publishing Group",
number = "7",

}

RIS

TY - JOUR

T1 - Structural and dynamic changes of photoactive yellow protein during its photocycle in solution

AU - Rubinstenn, G.

AU - Vuister, G. W.

AU - Mulder, F. A A

AU - Dux, P. E.

AU - Boelens, R.

AU - Hellingwerf, K. J.

AU - Kaptein, R.

PY - 1998/7/20

Y1 - 1998/7/20

N2 - 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.

AB - 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.

U2 - 10.1038/823

DO - 10.1038/823

M3 - Journal article

C2 - 9665170

AN - SCOPUS:0031821274

VL - 5

SP - 568

EP - 570

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

SN - 1545-9993

IS - 7

ER -