Automatic structure-based NMR methyl resonance assignment in large proteins

The structures and dynamics of large proteins can be studied with methyl-based NMR but peak assignment is still challenging. Here the authors present MethylFLYA that allows automated assignment of methyl groups and apply it to five proteins with molecular weights in the range from 28 to 358 kDa.

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Autores principales:	Iva Pritišanac, Julia M. Würz, T. Reid Alderson, Peter Güntert
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/a1784461fd9c43e19b12737b3b10db75
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spelling	oai:doaj.org-article:a1784461fd9c43e19b12737b3b10db752021-12-02T17:32:24ZAutomatic structure-based NMR methyl resonance assignment in large proteins10.1038/s41467-019-12837-82041-1723https://doaj.org/article/a1784461fd9c43e19b12737b3b10db752019-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-12837-8https://doaj.org/toc/2041-1723The structures and dynamics of large proteins can be studied with methyl-based NMR but peak assignment is still challenging. Here the authors present MethylFLYA that allows automated assignment of methyl groups and apply it to five proteins with molecular weights in the range from 28 to 358 kDa.Iva PritišanacJulia M. WürzT. Reid AldersonPeter GüntertNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Iva Pritišanac Julia M. Würz T. Reid Alderson Peter Güntert Automatic structure-based NMR methyl resonance assignment in large proteins
description	The structures and dynamics of large proteins can be studied with methyl-based NMR but peak assignment is still challenging. Here the authors present MethylFLYA that allows automated assignment of methyl groups and apply it to five proteins with molecular weights in the range from 28 to 358 kDa.
format	article
author	Iva Pritišanac Julia M. Würz T. Reid Alderson Peter Güntert
author_facet	Iva Pritišanac Julia M. Würz T. Reid Alderson Peter Güntert
author_sort	Iva Pritišanac
title	Automatic structure-based NMR methyl resonance assignment in large proteins
title_short	Automatic structure-based NMR methyl resonance assignment in large proteins
title_full	Automatic structure-based NMR methyl resonance assignment in large proteins
title_fullStr	Automatic structure-based NMR methyl resonance assignment in large proteins
title_full_unstemmed	Automatic structure-based NMR methyl resonance assignment in large proteins
title_sort	automatic structure-based nmr methyl resonance assignment in large proteins
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/a1784461fd9c43e19b12737b3b10db75
work_keys_str_mv	AT ivapritisanac automaticstructurebasednmrmethylresonanceassignmentinlargeproteins AT juliamwurz automaticstructurebasednmrmethylresonanceassignmentinlargeproteins AT treidalderson automaticstructurebasednmrmethylresonanceassignmentinlargeproteins AT peterguntert automaticstructurebasednmrmethylresonanceassignmentinlargeproteins
_version_	1718380324912627712

Automatic structure-based NMR methyl resonance assignment in large proteins

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