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Automatic structure-based NMR methyl resonance assignment in large proteins

Automatic structure-based NMR methyl resonance assignment in large proteins

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_a1784461fd9c43e19b12737b3b10db75

Automatic structure-based NMR methyl resonance assignment in large proteins

About this item

Full title

Automatic structure-based NMR methyl resonance assignment in large proteins

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2019-10, Vol.10 (1), p.4922-12, Article 4922

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Isotopically labeled methyl groups provide NMR probes in large, otherwise deuterated proteins. However, the resonance assignment constitutes a bottleneck for broader applicability of methyl-based NMR. Here, we present the automated MethylFLYA method for the assignment of methyl groups that is based on methyl-methyl nuclear Overhauser effect spectro...

Alternative Titles

Full title

Automatic structure-based NMR methyl resonance assignment in large proteins

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_a1784461fd9c43e19b12737b3b10db75

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_a1784461fd9c43e19b12737b3b10db75

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-019-12837-8

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