Resolving dynamics and function of transient states in single enzyme molecules

T4 Lysozyme (T4L) is a model protein whose structure is extensively studied. Here the authors combine single-molecule and ensemble FRET measurements, FRET-positioning and screening and EPR spectroscopy to study the structural dynamics of T4L and describe its conformational landscape during the catal...

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Autores principales:	Hugo Sanabria, Dmitro Rodnin, Katherina Hemmen, Thomas-Otavio Peulen, Suren Felekyan, Mark R. Fleissner, Mykola Dimura, Felix Koberling, Ralf Kühnemuth, Wayne Hubbell, Holger Gohlke, Claus A. M. Seidel
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/ac5a713e761c4aa39bb9d667d450bea4
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spelling	oai:doaj.org-article:ac5a713e761c4aa39bb9d667d450bea42021-12-02T15:37:13ZResolving dynamics and function of transient states in single enzyme molecules10.1038/s41467-020-14886-w2041-1723https://doaj.org/article/ac5a713e761c4aa39bb9d667d450bea42020-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-14886-whttps://doaj.org/toc/2041-1723T4 Lysozyme (T4L) is a model protein whose structure is extensively studied. Here the authors combine single-molecule and ensemble FRET measurements, FRET-positioning and screening and EPR spectroscopy to study the structural dynamics of T4L and describe its conformational landscape during the catalytic cycle by an extended Michaelis–Menten mechanism and identify an excited conformational state of the enzyme.Hugo SanabriaDmitro RodninKatherina HemmenThomas-Otavio PeulenSuren FelekyanMark R. FleissnerMykola DimuraFelix KoberlingRalf KühnemuthWayne HubbellHolger GohlkeClaus A. M. SeidelNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Hugo Sanabria Dmitro Rodnin Katherina Hemmen Thomas-Otavio Peulen Suren Felekyan Mark R. Fleissner Mykola Dimura Felix Koberling Ralf Kühnemuth Wayne Hubbell Holger Gohlke Claus A. M. Seidel Resolving dynamics and function of transient states in single enzyme molecules
description	T4 Lysozyme (T4L) is a model protein whose structure is extensively studied. Here the authors combine single-molecule and ensemble FRET measurements, FRET-positioning and screening and EPR spectroscopy to study the structural dynamics of T4L and describe its conformational landscape during the catalytic cycle by an extended Michaelis–Menten mechanism and identify an excited conformational state of the enzyme.
format	article
author	Hugo Sanabria Dmitro Rodnin Katherina Hemmen Thomas-Otavio Peulen Suren Felekyan Mark R. Fleissner Mykola Dimura Felix Koberling Ralf Kühnemuth Wayne Hubbell Holger Gohlke Claus A. M. Seidel
author_facet	Hugo Sanabria Dmitro Rodnin Katherina Hemmen Thomas-Otavio Peulen Suren Felekyan Mark R. Fleissner Mykola Dimura Felix Koberling Ralf Kühnemuth Wayne Hubbell Holger Gohlke Claus A. M. Seidel
author_sort	Hugo Sanabria
title	Resolving dynamics and function of transient states in single enzyme molecules
title_short	Resolving dynamics and function of transient states in single enzyme molecules
title_full	Resolving dynamics and function of transient states in single enzyme molecules
title_fullStr	Resolving dynamics and function of transient states in single enzyme molecules
title_full_unstemmed	Resolving dynamics and function of transient states in single enzyme molecules
title_sort	resolving dynamics and function of transient states in single enzyme molecules
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/ac5a713e761c4aa39bb9d667d450bea4
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_version_	1718386251376099328

Resolving dynamics and function of transient states in single enzyme molecules

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