Automatic structure-based NMR methyl resonance assignment in large proteins

Iva Pritišanac; Julia M. Würz; T. Reid Alderson; Peter Güntert

doi:10.1038/s41467-019-12837-8

Nature Communications (Oct 2019)

Automatic structure-based NMR methyl resonance assignment in large proteins

Iva Pritišanac,
Julia M. Würz,
T. Reid Alderson,
Peter Güntert

Affiliations

Iva Pritišanac: Institute of Biophysical Chemistry, Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt am Main
Julia M. Würz: Institute of Biophysical Chemistry, Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt am Main
T. Reid Alderson: Laboratory of Chemical Physics, NIDDK, National Institutes of Health
Peter Güntert: Institute of Biophysical Chemistry, Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt am Main

DOI: https://doi.org/10.1038/s41467-019-12837-8
Journal volume & issue: Vol. 10, no. 1
pp. 1 – 12

Abstract

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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.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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