Aucharova, HannaKlein, AlexanderMedina Gomez, SaraSöldner, BenediktVasa, Suresh K.Linser, Rasmus2025-09-092025-09-092024-02-21http://hdl.handle.net/2003/43873With 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.enChemical communications; 60(22)http://creativecommons.org/licenses/by/3.0/540Protein deuteration via algal amino acids to circumvent proton back-exchange for 1H-detected solid-state NMRArticle