Structural resolution of switchable states of a de novo peptide assembly

So far most of the de novo designed proteins are for single states only. Here, the authors present the de novo design and crystal structure determination of a coiled-coil peptide that assembles into multiple, distinct conformational states under the same conditions and further characterise its prope...

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Autores principales:	William M. Dawson, Eric J. M. Lang, Guto G. Rhys, Kathryn L. Shelley, Christopher Williams, R. Leo Brady, Matthew P. Crump, Adrian J. Mulholland, Derek N. Woolfson
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/da6fbe49cbb74470820dc44739bd5079
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spelling	oai:doaj.org-article:da6fbe49cbb74470820dc44739bd50792021-12-02T13:14:59ZStructural resolution of switchable states of a de novo peptide assembly10.1038/s41467-021-21851-82041-1723https://doaj.org/article/da6fbe49cbb74470820dc44739bd50792021-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-21851-8https://doaj.org/toc/2041-1723So far most of the de novo designed proteins are for single states only. Here, the authors present the de novo design and crystal structure determination of a coiled-coil peptide that assembles into multiple, distinct conformational states under the same conditions and further characterise its properties with biophysical experiments, NMR and MD simulations.William M. DawsonEric J. M. LangGuto G. RhysKathryn L. ShelleyChristopher WilliamsR. Leo BradyMatthew P. CrumpAdrian J. MulhollandDerek N. WoolfsonNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q William M. Dawson Eric J. M. Lang Guto G. Rhys Kathryn L. Shelley Christopher Williams R. Leo Brady Matthew P. Crump Adrian J. Mulholland Derek N. Woolfson Structural resolution of switchable states of a de novo peptide assembly
description	So far most of the de novo designed proteins are for single states only. Here, the authors present the de novo design and crystal structure determination of a coiled-coil peptide that assembles into multiple, distinct conformational states under the same conditions and further characterise its properties with biophysical experiments, NMR and MD simulations.
format	article
author	William M. Dawson Eric J. M. Lang Guto G. Rhys Kathryn L. Shelley Christopher Williams R. Leo Brady Matthew P. Crump Adrian J. Mulholland Derek N. Woolfson
author_facet	William M. Dawson Eric J. M. Lang Guto G. Rhys Kathryn L. Shelley Christopher Williams R. Leo Brady Matthew P. Crump Adrian J. Mulholland Derek N. Woolfson
author_sort	William M. Dawson
title	Structural resolution of switchable states of a de novo peptide assembly
title_short	Structural resolution of switchable states of a de novo peptide assembly
title_full	Structural resolution of switchable states of a de novo peptide assembly
title_fullStr	Structural resolution of switchable states of a de novo peptide assembly
title_full_unstemmed	Structural resolution of switchable states of a de novo peptide assembly
title_sort	structural resolution of switchable states of a de novo peptide assembly
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/da6fbe49cbb74470820dc44739bd5079
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Structural resolution of switchable states of a de novo peptide assembly

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