Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy

Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy

Analysis of side-chain motions by NMR has so far been restricted to small proteins and methyl-bearing side chains. Here, the authors present NMR methods based on 13C direct detection of highly deuterated protein samples that yield sharp and well-resolved signals and allow the characterisation of sid...

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Main Authors: Ruth B. Pritchard, D. Flemming Hansen
Format: Article
Language:English
Published: Nature Publishing Group 2019-04-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-019-09743-4
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spelling doaj-0da10a54a94e459fb2afae5adb60909a2021-05-11T12:05:43ZengNature Publishing GroupNature Communications2041-17232019-04-011011710.1038/s41467-019-09743-4Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopyRuth B. Pritchard0D. Flemming Hansen1Institute of Structural and Molecular Biology, Division of Biosciences, University College LondonInstitute of Structural and Molecular Biology, Division of Biosciences, University College LondonAnalysis of side-chain motions by NMR has so far been restricted to small proteins and methyl-bearing side chains. Here, the authors present NMR methods based on 13C direct detection of highly deuterated protein samples that yield sharp and well-resolved signals and allow the characterisation of side-chain conformational dynamics of six different amino acid types in medium-to-large proteins.https://doi.org/10.1038/s41467-019-09743-4
collection DOAJ
language English
format Article
sources DOAJ
author Ruth B. Pritchard
D. Flemming Hansen
spellingShingle Ruth B. Pritchard
D. Flemming Hansen
Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy
Nature Communications
author_facet Ruth B. Pritchard
D. Flemming Hansen
author_sort Ruth B. Pritchard
title Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy
title_short Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy
title_full Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy
title_fullStr Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy
title_full_unstemmed Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy
title_sort characterising side chains in large proteins by protonless 13c-detected nmr spectroscopy
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2019-04-01
description Analysis of side-chain motions by NMR has so far been restricted to small proteins and methyl-bearing side chains. Here, the authors present NMR methods based on 13C direct detection of highly deuterated protein samples that yield sharp and well-resolved signals and allow the characterisation of side-chain conformational dynamics of six different amino acid types in medium-to-large proteins.
url https://doi.org/10.1038/s41467-019-09743-4
work_keys_str_mv AT ruthbpritchard characterisingsidechainsinlargeproteinsbyprotonless13cdetectednmrspectroscopy
AT dflemminghansen characterisingsidechainsinlargeproteinsbyprotonless13cdetectednmrspectroscopy
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