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bioRxiv · 10.1101/2024.01.07.574532

Protein deuteration via algal amino acids to overcome proton back-exchange for fast-MAS solid-state NMR of large proteins

Aucharova, H.·Klein, A.·Medina Gomez, S.·Soeldner, B.·Vasa, S. K.·Linser, R.
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Abstract

With perdeuteration, a current standard for solid-state NMR spectroscopy, large proteins suffer from incomplete amide-proton back-exchange. Using a 72 kDa micro-crystalline protein, we show that deuteration exclusively via deuterated amino acids, largely suppressing sidechain protonation, provides spectral resolution comparable to perdeuterated preparations at intermediate spinning frequencies without proton back-exchange obstacles.

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Aucharova, H., Klein, A., Medina Gomez, S., Soeldner, B., Vasa, S. K., Linser, R.. 2024-01-07. Protein deuteration via algal amino acids to overcome proton back-exchange for fast-MAS solid-state NMR of large proteins. https://doi.org/10.1101/2024.01.07.574532

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