Protein deuteration via algal amino acids to circumvent proton back-exchange for 1H-detected solid-state NMR

With perdeuteration, solid-state NMR spectroscopy of large proteins suffers from incomplete amide-proton back-exchange. Using a 72 kDa micro-crystalline protein, we show that deuteration exclusively via deuterated amino acids, well-established in solution to suppress sidechain protonation without pr...

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Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2024-03, Vol.60 (22), p.3083-3086
Main Authors: Aucharova, Hanna, Klein, Alexander, Sara Medina Gomez, Söldner, Benedikt, Vasa, Suresh K, Linser, Rasmus
Format: Article
Language:English
Subjects:
Amino acids
Chemistry
Deuteration
Exchanging
NMR spectroscopy
Proteins
Protonation
Protons
Solid state
Spectral resolution
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Summary:With perdeuteration, solid-state NMR spectroscopy of large proteins suffers from incomplete amide-proton back-exchange. Using a 72 kDa micro-crystalline protein, we show that deuteration exclusively via deuterated amino acids, well-established in solution to suppress sidechain protonation without proton back-exchange obstacles, provides spectral resolution comparable to perdeuterated preparations at intermediate spinning frequencies.
ISSN:1359-7345
1364-548X
1364-548X
DOI:10.1039/d4cc00213j