Confinement in crystal lattice alters entire photocycle pathway of the Photoactive Yellow Protein

Protein structural dynamics can be studied by time-resolved crystallography (TRC) and ultrafast transient spectroscopic methods. Here, the authors perform electronic and vibrational transient absorption measurements to characterise the full photocycle of Photoactive Yellow Protein (PYP) both in the...

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Autores principales:	Patrick E. Konold, Enis Arik, Jörn Weißenborn, Jos C. Arents, Klaas J. Hellingwerf, Ivo H. M. van Stokkum, John T. M. Kennis, Marie Louise Groot
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/2f846740cfbb4428b7a602dd2a81f7d1
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spelling	oai:doaj.org-article:2f846740cfbb4428b7a602dd2a81f7d12021-12-02T18:53:11ZConfinement in crystal lattice alters entire photocycle pathway of the Photoactive Yellow Protein10.1038/s41467-020-18065-92041-1723https://doaj.org/article/2f846740cfbb4428b7a602dd2a81f7d12020-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-18065-9https://doaj.org/toc/2041-1723Protein structural dynamics can be studied by time-resolved crystallography (TRC) and ultrafast transient spectroscopic methods. Here, the authors perform electronic and vibrational transient absorption measurements to characterise the full photocycle of Photoactive Yellow Protein (PYP) both in the crystalline and solution state and find that the photocycle kinetics and structural intermediates of PYP deviate in the crystalline state, which must be taken into consideration when planning TRC experiments.Patrick E. KonoldEnis ArikJörn WeißenbornJos C. ArentsKlaas J. HellingwerfIvo H. M. van StokkumJohn T. M. KennisMarie Louise GrootNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Patrick E. Konold Enis Arik Jörn Weißenborn Jos C. Arents Klaas J. Hellingwerf Ivo H. M. van Stokkum John T. M. Kennis Marie Louise Groot Confinement in crystal lattice alters entire photocycle pathway of the Photoactive Yellow Protein
description	Protein structural dynamics can be studied by time-resolved crystallography (TRC) and ultrafast transient spectroscopic methods. Here, the authors perform electronic and vibrational transient absorption measurements to characterise the full photocycle of Photoactive Yellow Protein (PYP) both in the crystalline and solution state and find that the photocycle kinetics and structural intermediates of PYP deviate in the crystalline state, which must be taken into consideration when planning TRC experiments.
format	article
author	Patrick E. Konold Enis Arik Jörn Weißenborn Jos C. Arents Klaas J. Hellingwerf Ivo H. M. van Stokkum John T. M. Kennis Marie Louise Groot
author_facet	Patrick E. Konold Enis Arik Jörn Weißenborn Jos C. Arents Klaas J. Hellingwerf Ivo H. M. van Stokkum John T. M. Kennis Marie Louise Groot
author_sort	Patrick E. Konold
title	Confinement in crystal lattice alters entire photocycle pathway of the Photoactive Yellow Protein
title_short	Confinement in crystal lattice alters entire photocycle pathway of the Photoactive Yellow Protein
title_full	Confinement in crystal lattice alters entire photocycle pathway of the Photoactive Yellow Protein
title_fullStr	Confinement in crystal lattice alters entire photocycle pathway of the Photoactive Yellow Protein
title_full_unstemmed	Confinement in crystal lattice alters entire photocycle pathway of the Photoactive Yellow Protein
title_sort	confinement in crystal lattice alters entire photocycle pathway of the photoactive yellow protein
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/2f846740cfbb4428b7a602dd2a81f7d1
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Confinement in crystal lattice alters entire photocycle pathway of the Photoactive Yellow Protein

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