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  1H-Detected Biomolecular NMR under Fast Magic-Angle Spinning

Le Marchand, T., Schubeis, T., Bonaccorsi, M., Paluch, P., Lalli, D., Pell, A. J., et al. (2022). 1H-Detected Biomolecular NMR under Fast Magic-Angle Spinning. Chemical Reviews, 122(10), 9943-10018. doi:10.1021/acs.chemrev.1c00918.

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Genre: Journal Article
Other : H-1-Detected Biomolecular NMR under Fast Magic-Angle Spinning
Other : 1H-Detected Biomolecular NMR under Fast Magic-Angle Spinning


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Le Marchand, Tanguy, Author
Schubeis, Tobias, Author
Bonaccorsi, Marta, Author
Paluch, Piotr, Author
Lalli, Daniela, Author
Pell, Andrew J., Author
Andreas, Loren B.1, Author           
Jaudzems, Kristaps, Author
Stanek, Jan, Author
Pintacuda, Guido, Author
1Department of NMR Based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society, ou_3350124              


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 Abstract: Since the first pioneering studies on small deuterated peptides dating more than 20 years ago, 1H detection has evolved into the most efficient approach for investigation of biomolecular structure, dynamics, and interactions by solid-state NMR. The development of faster and faster magic-angle spinning (MAS) rates (up to 150 kHz today) at ultrahigh magnetic fields has triggered a real revolution in the field. This new spinning regime reduces the 1H-1H dipolar couplings, so that a direct detection of 1H signals, for long impossible without proton dilution, has become possible at high resolution. The switch from the traditional MAS NMR approaches with 13C and 15N detection to 1H boosts the signal by more than an order of magnitude, accelerating the site-specific analysis and opening the way to more complex immobilized biological systems of higher molecular weight and available in limited amounts. This paper reviews the concepts underlying this recent leap forward in sensitivity and resolution, presents a detailed description of the experimental aspects of acquisition of multidimensional correlation spectra with fast MAS, and summarizes the most successful strategies for the assignment of the resonances and for the elucidation of protein structure and conformational dynamics. It finally outlines the many examples where 1H-detected MAS NMR has contributed to the detailed characterization of a variety of crystalline and noncrystalline biomolecular targets involved in biological processes ranging from catalysis through drug binding, viral infectivity, amyloid fibril formation, to transport across lipid membranes.


Language(s): eng - English
 Dates: 2022-05-102022
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/acs.chemrev.1c00918
 Degree: -



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Project name : The development of biomolecular 1H-detected NMR in Lyon has been funded over the past few years by the European Research Council (ERC) under the European Union’s Horizon 2020 research and innovation programme (ERC-2015-CoG GA 648974 to G.P.), by the European Union’s FP7 research and innovation programme (FP7-PEOPLE-2012-ITN GA 317127 to G.P.), by joint research activities and transnational access within the consortia (Infrastructure for NMR, EM, and X-rays for Translational Research, GA 653706) and iNext Discovery (Structural biology for Translational Research and Discovery, GA 871037), by the Institut de Chimie de Lyon (FR3023) and by the CNRS (IR-RMN-THC FR3050 and Infranalytics FR2054). The computational resources for the simulations reported in this work were provided by the Polish Infrastructure for Supporting Computational Science in the European Research Space (PLGRID, grant ID: plgnmrsi2). J.S. and P.P. are supported by the Polish National Agency for Academic Exchange in the framework of Polish Return programme (Contract No. PPN/PPO/2018/1/00098). K.J. is supported by Latvian Council of Science Grant No. lzp-2019/1-0244. L.B.A.’s research group is supported by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) through the Emmy Noether Program (Grant AN1316/1-1) and project A04 of the SFB 803.
Grant ID : -
Funding program : -
Funding organization : -
Project name : ERC-2015-CoG GA
Grant ID : 648974
Funding program : Horizon 2020 (H2020)
Funding organization : European Commission (EC)
Project name : European Union’s FP7 research and innovation programme
Grant ID : 317127
Funding program : European Union’s FP7 (FP7-PEOPLE-2012-ITN)
Funding organization : European Commission (EC)

Source 1

Title: Chemical Reviews
  Abbreviation : Chem. Rev.
Source Genre: Journal
Publ. Info: Washington, DC. : American Chemical Society
Pages: - Volume / Issue: 122 (10) Sequence Number: - Start / End Page: 9943 - 10018 Identifier: ISSN: 0009-2665
CoNE: https://pure.mpg.de/cone/journals/resource/954925389243