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

被引:0
作者
Aucharova, Hanna [1 ]
Klein, Alexander [1 ]
Gomez, Sara Medina [1 ]
Soeldner, Benedikt [1 ]
Vasa, Suresh K. [1 ]
Linser, Rasmus [1 ]
机构
[1] TU Dortmund Univ, Dept Chem & Chem Biol Biophys Chem, Otto Hahn Str 4a, D-44227 Dortmund, Germany
基金
欧洲研究理事会;
关键词
MEMBRANE-PROTEINS; SPECTROSCOPY;
D O I
10.1039/d4cc00213j
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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.
引用
收藏
页码:3083 / 3086
页数:4
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