Accurate protein structure prediction with hydroxyl radical protein footprinting data

Mass spectrometry-based covalent labeling techniques such as hydroxyl radical protein footprinting (HRPF) provide information about protein tertiary structures. Here, the authors present a dynamics driven HRPF-guided algorithm for protein structure prediction that is incorporated in the Rosetta soft...

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Autores principales:	Sarah E. Biehn, Steffen Lindert
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/5037b04e13a0484696d053dec74e8923
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id	oai:doaj.org-article:5037b04e13a0484696d053dec74e8923
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spelling	oai:doaj.org-article:5037b04e13a0484696d053dec74e89232021-12-02T14:11:45ZAccurate protein structure prediction with hydroxyl radical protein footprinting data10.1038/s41467-020-20549-72041-1723https://doaj.org/article/5037b04e13a0484696d053dec74e89232021-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-20549-7https://doaj.org/toc/2041-1723Mass spectrometry-based covalent labeling techniques such as hydroxyl radical protein footprinting (HRPF) provide information about protein tertiary structures. Here, the authors present a dynamics driven HRPF-guided algorithm for protein structure prediction that is incorporated in the Rosetta software suite and only requires the protein sequence and HRPF data as input and they demonstrate its successful application to four benchmark proteins.Sarah E. BiehnSteffen LindertNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Sarah E. Biehn Steffen Lindert Accurate protein structure prediction with hydroxyl radical protein footprinting data
description	Mass spectrometry-based covalent labeling techniques such as hydroxyl radical protein footprinting (HRPF) provide information about protein tertiary structures. Here, the authors present a dynamics driven HRPF-guided algorithm for protein structure prediction that is incorporated in the Rosetta software suite and only requires the protein sequence and HRPF data as input and they demonstrate its successful application to four benchmark proteins.
format	article
author	Sarah E. Biehn Steffen Lindert
author_facet	Sarah E. Biehn Steffen Lindert
author_sort	Sarah E. Biehn
title	Accurate protein structure prediction with hydroxyl radical protein footprinting data
title_short	Accurate protein structure prediction with hydroxyl radical protein footprinting data
title_full	Accurate protein structure prediction with hydroxyl radical protein footprinting data
title_fullStr	Accurate protein structure prediction with hydroxyl radical protein footprinting data
title_full_unstemmed	Accurate protein structure prediction with hydroxyl radical protein footprinting data
title_sort	accurate protein structure prediction with hydroxyl radical protein footprinting data
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/5037b04e13a0484696d053dec74e8923
work_keys_str_mv	AT sarahebiehn accurateproteinstructurepredictionwithhydroxylradicalproteinfootprintingdata AT steffenlindert accurateproteinstructurepredictionwithhydroxylradicalproteinfootprintingdata
_version_	1718391841022279680

Accurate protein structure prediction with hydroxyl radical protein footprinting data

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