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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.

2024-01-07 biochemistry
10.1101/2024.01.07.574532 bioRxiv
Show 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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