Diselenide crosslinks for enhanced and simplified oxidative protein folding

Hirudin is a widely studied model for folding of disulfide-rich proteins, which folds through a slow pathway with highly heterogeneous intermediates and scrambled isomers before it reaches its native state. Here the effect of native and non-native diselenide bridges on the kinetics, yield, and heter...

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Autores principales:	Reem Mousa, Taghreed Hidmi, Sergei Pomyalov, Shifra Lansky, Lareen Khouri, Deborah E. Shalev, Gil Shoham, Norman Metanis
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/90ff74c53b084ca3a7d24d11009d7db6
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spelling	oai:doaj.org-article:90ff74c53b084ca3a7d24d11009d7db62021-12-02T13:33:00ZDiselenide crosslinks for enhanced and simplified oxidative protein folding10.1038/s42004-021-00463-92399-3669https://doaj.org/article/90ff74c53b084ca3a7d24d11009d7db62021-03-01T00:00:00Zhttps://doi.org/10.1038/s42004-021-00463-9https://doaj.org/toc/2399-3669Hirudin is a widely studied model for folding of disulfide-rich proteins, which folds through a slow pathway with highly heterogeneous intermediates and scrambled isomers before it reaches its native state. Here the effect of native and non-native diselenide bridges on the kinetics, yield, and heterogeneity of hirudin folding are systematically explored.Reem MousaTaghreed HidmiSergei PomyalovShifra LanskyLareen KhouriDeborah E. ShalevGil ShohamNorman MetanisNature PortfolioarticleChemistryQD1-999ENCommunications Chemistry, Vol 4, Iss 1, Pp 1-9 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Chemistry QD1-999
spellingShingle	Chemistry QD1-999 Reem Mousa Taghreed Hidmi Sergei Pomyalov Shifra Lansky Lareen Khouri Deborah E. Shalev Gil Shoham Norman Metanis Diselenide crosslinks for enhanced and simplified oxidative protein folding
description	Hirudin is a widely studied model for folding of disulfide-rich proteins, which folds through a slow pathway with highly heterogeneous intermediates and scrambled isomers before it reaches its native state. Here the effect of native and non-native diselenide bridges on the kinetics, yield, and heterogeneity of hirudin folding are systematically explored.
format	article
author	Reem Mousa Taghreed Hidmi Sergei Pomyalov Shifra Lansky Lareen Khouri Deborah E. Shalev Gil Shoham Norman Metanis
author_facet	Reem Mousa Taghreed Hidmi Sergei Pomyalov Shifra Lansky Lareen Khouri Deborah E. Shalev Gil Shoham Norman Metanis
author_sort	Reem Mousa
title	Diselenide crosslinks for enhanced and simplified oxidative protein folding
title_short	Diselenide crosslinks for enhanced and simplified oxidative protein folding
title_full	Diselenide crosslinks for enhanced and simplified oxidative protein folding
title_fullStr	Diselenide crosslinks for enhanced and simplified oxidative protein folding
title_full_unstemmed	Diselenide crosslinks for enhanced and simplified oxidative protein folding
title_sort	diselenide crosslinks for enhanced and simplified oxidative protein folding
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/90ff74c53b084ca3a7d24d11009d7db6
work_keys_str_mv	AT reemmousa diselenidecrosslinksforenhancedandsimplifiedoxidativeproteinfolding AT taghreedhidmi diselenidecrosslinksforenhancedandsimplifiedoxidativeproteinfolding AT sergeipomyalov diselenidecrosslinksforenhancedandsimplifiedoxidativeproteinfolding AT shifralansky diselenidecrosslinksforenhancedandsimplifiedoxidativeproteinfolding AT lareenkhouri diselenidecrosslinksforenhancedandsimplifiedoxidativeproteinfolding AT deboraheshalev diselenidecrosslinksforenhancedandsimplifiedoxidativeproteinfolding AT gilshoham diselenidecrosslinksforenhancedandsimplifiedoxidativeproteinfolding AT normanmetanis diselenidecrosslinksforenhancedandsimplifiedoxidativeproteinfolding
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Diselenide crosslinks for enhanced and simplified oxidative protein folding

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