Large-scale discovery of protein interactions at residue resolution using co-evolution calculated from genomic sequences

Our understanding of the residue-level details of protein interactions remains incomplete. Here, the authors show sequence coevolution can be used to infer interacting proteins with residue-level details, including predicting 467 interactions de novo in the Escherichia coli cell envelope proteome.

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Autores principales:	Anna G. Green, Hadeer Elhabashy, Kelly P. Brock, Rohan Maddamsetti, Oliver Kohlbacher, Debora S. Marks
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/1f5d36246a5a4cf98d205592e87dd62a
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spelling	oai:doaj.org-article:1f5d36246a5a4cf98d205592e87dd62a2021-12-02T13:32:54ZLarge-scale discovery of protein interactions at residue resolution using co-evolution calculated from genomic sequences10.1038/s41467-021-21636-z2041-1723https://doaj.org/article/1f5d36246a5a4cf98d205592e87dd62a2021-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-21636-zhttps://doaj.org/toc/2041-1723Our understanding of the residue-level details of protein interactions remains incomplete. Here, the authors show sequence coevolution can be used to infer interacting proteins with residue-level details, including predicting 467 interactions de novo in the Escherichia coli cell envelope proteome.Anna G. GreenHadeer ElhabashyKelly P. BrockRohan MaddamsettiOliver KohlbacherDebora S. MarksNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Anna G. Green Hadeer Elhabashy Kelly P. Brock Rohan Maddamsetti Oliver Kohlbacher Debora S. Marks Large-scale discovery of protein interactions at residue resolution using co-evolution calculated from genomic sequences
description	Our understanding of the residue-level details of protein interactions remains incomplete. Here, the authors show sequence coevolution can be used to infer interacting proteins with residue-level details, including predicting 467 interactions de novo in the Escherichia coli cell envelope proteome.
format	article
author	Anna G. Green Hadeer Elhabashy Kelly P. Brock Rohan Maddamsetti Oliver Kohlbacher Debora S. Marks
author_facet	Anna G. Green Hadeer Elhabashy Kelly P. Brock Rohan Maddamsetti Oliver Kohlbacher Debora S. Marks
author_sort	Anna G. Green
title	Large-scale discovery of protein interactions at residue resolution using co-evolution calculated from genomic sequences
title_short	Large-scale discovery of protein interactions at residue resolution using co-evolution calculated from genomic sequences
title_full	Large-scale discovery of protein interactions at residue resolution using co-evolution calculated from genomic sequences
title_fullStr	Large-scale discovery of protein interactions at residue resolution using co-evolution calculated from genomic sequences
title_full_unstemmed	Large-scale discovery of protein interactions at residue resolution using co-evolution calculated from genomic sequences
title_sort	large-scale discovery of protein interactions at residue resolution using co-evolution calculated from genomic sequences
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/1f5d36246a5a4cf98d205592e87dd62a
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Large-scale discovery of protein interactions at residue resolution using co-evolution calculated from genomic sequences

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