Methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk

Spider silk is of interest in material science research. Here the authors show that the tight binding of a spider silk protein domain relies on the amino acid methionine, which is abundant in the domain core where it facilitates dynamic shape adaption of the binding interface.

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Autores principales:	Julia C. Heiby, Benedikt Goretzki, Christopher M. Johnson, Ute A. Hellmich, Hannes Neuweiler
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/cbb044ff25df467b8fda4b6d45554c9a
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spelling	oai:doaj.org-article:cbb044ff25df467b8fda4b6d45554c9a2021-12-02T17:02:00ZMethionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk10.1038/s41467-019-12365-52041-1723https://doaj.org/article/cbb044ff25df467b8fda4b6d45554c9a2019-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-12365-5https://doaj.org/toc/2041-1723Spider silk is of interest in material science research. Here the authors show that the tight binding of a spider silk protein domain relies on the amino acid methionine, which is abundant in the domain core where it facilitates dynamic shape adaption of the binding interface.Julia C. HeibyBenedikt GoretzkiChristopher M. JohnsonUte A. HellmichHannes NeuweilerNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Julia C. Heiby Benedikt Goretzki Christopher M. Johnson Ute A. Hellmich Hannes Neuweiler Methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk
description	Spider silk is of interest in material science research. Here the authors show that the tight binding of a spider silk protein domain relies on the amino acid methionine, which is abundant in the domain core where it facilitates dynamic shape adaption of the binding interface.
format	article
author	Julia C. Heiby Benedikt Goretzki Christopher M. Johnson Ute A. Hellmich Hannes Neuweiler
author_facet	Julia C. Heiby Benedikt Goretzki Christopher M. Johnson Ute A. Hellmich Hannes Neuweiler
author_sort	Julia C. Heiby
title	Methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk
title_short	Methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk
title_full	Methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk
title_fullStr	Methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk
title_full_unstemmed	Methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk
title_sort	methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/cbb044ff25df467b8fda4b6d45554c9a
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Methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk

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