Rapid Proton-Detected NMR Assignment for Proteins with Fast Magic Angle Spinning

被引:243
作者
Barbet-Massin, Emeline [1 ]
Pell, Andrew J. [1 ]
Retel, Joren S. [2 ]
Andreas, Loren B. [1 ,3 ,4 ]
Jaudzems, Kristaps [5 ]
Franks, W. Trent [2 ]
Nieuwkoop, Andrew J. [2 ]
Hiller, Matthias [2 ]
Higman, Victoria [2 ]
Guerry, Paul [1 ]
Bertarello, Andrea [1 ]
Knight, Michael J. [1 ]
Felletti, Michele [1 ]
Le Marchand, Tanguy [1 ]
Kotelovica, Svetlana [6 ]
Akopjana, Inara [6 ]
Tars, Kaspars [6 ]
Stoppini, Monica [7 ]
Bellotti, Vittorio [7 ,8 ]
Bolognesi, Martino [9 ]
Ricagno, Stefano [9 ]
Chou, James J. [10 ]
Griffin, Robert G. [3 ,4 ]
Oschkinat, Hartmut [2 ]
Lesage, Anne [1 ]
Emsley, Lyndon [1 ]
Herrmann, Torsten [1 ]
Pintacuda, Guido
机构
[1] Univ Lyon, Ctr RMN Tres Hauts Champs, Inst Sci Analyt, CNRS,ENS Lyon,UCB Lyon 1, F-69100 Villeurbanne, France
[2] Leibniz Inst Mol Pharmacol, D-13125 Berlin, Germany
[3] MIT, Francis Bitter Magnet Lab, Cambridge, MA 02139 USA
[4] MIT, Dept Chem, Cambridge, MA 02139 USA
[5] Latvian Inst Organ Synth, LV-1006 Riga, Latvia
[6] Biomed Res & Study Ctr, LV-1067 Riga, Latvia
[7] Univ Pavia, Dept Mol Med, I-65 Pavia, Italy
[8] UCL, Ctr Amyloidosis & Acute Phase Prot, Natl Amyloidosis Ctr, Wolfson Drug Discovery Ctr, London WC1E 6BT, England
[9] Univ Milan, Dept Biosci, I-20126 Milan, Italy
[10] Harvard Univ, Sch Med, Boston, MA 02115 USA
基金
美国国家科学基金会;
关键词
SOLID-STATE NMR; RESONANCE ASSIGNMENT; CORRELATION SPECTROSCOPY; AMYLOID FIBRILS; RESOLUTION; MAS; SEQUENCE; SPECTRA; POLARIZATION; H-1-NMR;
D O I
10.1021/ja507382j
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Using a set of six H-1-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 H-2/H-1 exchange, high magnetic fields, and high-spinning frequencies (omega(r)/2 pi >= 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 C-13/N-15-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.
引用
收藏
页码:12489 / 12497
页数:9
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