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EnglishUsing a set of six (1)H-detected triple-resonance NMR experiments, we establish a method for sequence-specific backbone resonance assignment of magic angle spinning (MAS) nuclear magnetic resonance (NMR) spectra of 5-30 kDa proteins. The approach relies on perdeuteration, amide (2)H/(1)H exchange, high magnetic fields, and high-spinning frequencies (ωr/2π ≥ 60 kHz) and yields high-quality NMR data, enabling the use of automated analysis. The method is validated with five examples of proteins in different condensed states, including two microcrystalline proteins, a sedimented virus capsid, and two membrane-embedded systems. In comparison to contemporary (13)C/(15)N-based methods, this approach facilitates and accelerates the MAS NMR assignment process, shortening the spectral acquisition times and enabling the use of unsupervised state-of-the-art computational data analysis protocols originally developed for solution NMR.
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| Titolo: | Rapid proton-detected NMR assignment for proteins with fast magic angle spinning. |
| Autori: | |
| Data di pubblicazione: | 2014 |
| Rivista: | |
| Citazione: | Rapid proton-detected NMR assignment for proteins with fast magic angle spinning. / Barbet-Massin E;Pell AJ;Retel JS;Andreas LB;Jaudzems K;Franks WT;Nieuwkoop AJ;Hiller M;Higman V;Guerry P;Bertarello A;Knight MJ;Felletti M;Le Marchand T;Kotelovica S;Akopjana I;Tars K;Stoppini M;Bellotti V;Bolognesi M;Ricagno S;Chou JJ;Griffin RG;Oschkinat H;Lesage A;Emsley L;Herrmann T;Pintacuda G. - In: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY. - ISSN 0002-7863. - STAMPA. - 136:35(2014), pp. 12489-12497. |
| Abstract: | Using a set of six (1)H-detected triple-resonance NMR experiments, we establish a method for sequence-specific backbone resonance assignment of magic angle spinning (MAS) nuclear magnetic resonance (NMR) spectra of 5-30 kDa proteins. The approach relies on perdeuteration, amide (2)H/(1)H exchange, high magnetic fields, and high-spinning frequencies (ωr/2π ≥ 60 kHz) and yields high-quality NMR data, enabling the use of automated analysis. The method is validated with five examples of proteins in different condensed states, including two microcrystalline proteins, a sedimented virus capsid, and two membrane-embedded systems. In comparison to contemporary (13)C/(15)N-based methods, this approach facilitates and accelerates the MAS NMR assignment process, shortening the spectral acquisition times and enabling the use of unsupervised state-of-the-art computational data analysis protocols originally developed for solution NMR. |
| Handle: | http://hdl.handle.net/11571/954234 |
| Appare nelle tipologie: | 1.1 Articolo in rivista |
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