Subnanometre enzyme mechanics probed by single-molecule force spectroscopy

Adenylate kinase catalyses the interconversion of adenosine phosphates, and plays a crucial role in maintaining cellular energy homeostasis. Here, the authors use single molecule optical tweezers to understand how the enzyme’s conformation dynamics modulates catalysis.

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Autores principales:	Benjamin Pelz, Gabriel Žoldák, Fabian Zeller, Martin Zacharias, Matthias Rief
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/f4fe9840fe134709ad725d0e0b555534
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spelling	oai:doaj.org-article:f4fe9840fe134709ad725d0e0b5555342021-12-02T15:34:09ZSubnanometre enzyme mechanics probed by single-molecule force spectroscopy10.1038/ncomms108482041-1723https://doaj.org/article/f4fe9840fe134709ad725d0e0b5555342016-02-01T00:00:00Zhttps://doi.org/10.1038/ncomms10848https://doaj.org/toc/2041-1723Adenylate kinase catalyses the interconversion of adenosine phosphates, and plays a crucial role in maintaining cellular energy homeostasis. Here, the authors use single molecule optical tweezers to understand how the enzyme’s conformation dynamics modulates catalysis.Benjamin PelzGabriel ŽoldákFabian ZellerMartin ZachariasMatthias RiefNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-9 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Benjamin Pelz Gabriel Žoldák Fabian Zeller Martin Zacharias Matthias Rief Subnanometre enzyme mechanics probed by single-molecule force spectroscopy
description	Adenylate kinase catalyses the interconversion of adenosine phosphates, and plays a crucial role in maintaining cellular energy homeostasis. Here, the authors use single molecule optical tweezers to understand how the enzyme’s conformation dynamics modulates catalysis.
format	article
author	Benjamin Pelz Gabriel Žoldák Fabian Zeller Martin Zacharias Matthias Rief
author_facet	Benjamin Pelz Gabriel Žoldák Fabian Zeller Martin Zacharias Matthias Rief
author_sort	Benjamin Pelz
title	Subnanometre enzyme mechanics probed by single-molecule force spectroscopy
title_short	Subnanometre enzyme mechanics probed by single-molecule force spectroscopy
title_full	Subnanometre enzyme mechanics probed by single-molecule force spectroscopy
title_fullStr	Subnanometre enzyme mechanics probed by single-molecule force spectroscopy
title_full_unstemmed	Subnanometre enzyme mechanics probed by single-molecule force spectroscopy
title_sort	subnanometre enzyme mechanics probed by single-molecule force spectroscopy
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/f4fe9840fe134709ad725d0e0b555534
work_keys_str_mv	AT benjaminpelz subnanometreenzymemechanicsprobedbysinglemoleculeforcespectroscopy AT gabrielzoldak subnanometreenzymemechanicsprobedbysinglemoleculeforcespectroscopy AT fabianzeller subnanometreenzymemechanicsprobedbysinglemoleculeforcespectroscopy AT martinzacharias subnanometreenzymemechanicsprobedbysinglemoleculeforcespectroscopy AT matthiasrief subnanometreenzymemechanicsprobedbysinglemoleculeforcespectroscopy
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Subnanometre enzyme mechanics probed by single-molecule force spectroscopy

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