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

来源：

CHEMICAL COMMUNICATIONS | 2024年 / 60卷 / 22期

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

页码：3083 / 3086

页数：4

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