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Protein deuteration via algal amino acids to circumvent proton back-exchange for 1H-detected solid-state NMR.
- Source :
-
Chemical Communications . 3/18/2024, Vol. 60 Issue 22, p3083-3086. 4p. - Publication Year :
- 2024
-
Abstract
- 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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 13597345
- Volume :
- 60
- Issue :
- 22
- Database :
- Academic Search Index
- Journal :
- Chemical Communications
- Publication Type :
- Academic Journal
- Accession number :
- 175992796
- Full Text :
- https://doi.org/10.1039/d4cc00213j