Articles | Volume 5, issue 1
https://doi.org/10.5194/mr-5-33-2024
https://doi.org/10.5194/mr-5-33-2024
Research article
 | 
19 Apr 2024
Research article |  | 19 Apr 2024

Deuteration of proteins boosted by cell lysates: high-resolution amide and Hα magic-angle-spinning (MAS) NMR without the reprotonation bottleneck

Federico Napoli, Jia-Ying Guan, Charles-Adrien Arnaud, Pavel Macek, Hugo Fraga, Cécile Breyton, and Paul Schanda

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Cited articles

Agarwal, V., Penzel, S., Szekely, K., Cadalbert, R., Testori, E., Oss, A., Past, J., Samoson, A., Ernst, M., Böckmann, A., and Meier, B. H.: De novo 3D structure determination from sub-milligram protein samples by solid-state 100 kHz MAS NMR spectroscopy, Angew. Chem. Int. Edit., 53, 12253–12256, 2014. a
Anderson, E.: Growth requirements of virus-resistant mutants of Escherichia coli strain “B”, P. Natl. Acad. Sci. USA, 32, 120–128, 1946. a
Arnaud, C.-A., Effantin, G., Vivès, C., Engilberge, S., Bacia, M., Boulanger, P., Girard, E., Schoehn, G., and Breyton, C.: Bacteriophage T5 tail tube structure suggests a trigger mechanism for Siphoviridae DNA ejection, Nat. Commun., 8, 1953, https://doi.org/10.1038/s41467-017-02049-3, 2017. a
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Short summary
Protons (1H) are useful reporters of protein structure and dynamics in solid-state NMR. However, 1H abundance is detrimental to the resolution of NMR spectra. Substituting 1H by deuterons has been an efficient strategy to improve spectral quality, but when the crucial backbone amide sites are not protonated, much information is loss. We propose a method to completely protonate the amide sites, while maintaining high-resolution information, which partially also extends to backbone alpha-1H.