Biomolecular solid-state NMR spectroscopy at 1200 MHz: the gain in resolution


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Date

2021-07

Publication Type

Journal Article

ETH Bibliography

yes

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Data

Abstract

Progress in NMR in general and in biomolecular applications in particular is driven by increasing magnetic-field strengths leading to improved resolution and sensitivity of the NMR spectra. Recently, persistent superconducting magnets at a magnetic field strength (magnetic induction) of 28.2 T corresponding to 1200 MHz proton resonance frequency became commercially available. We present here a collection of high-field NMR spectra of a variety of proteins, including molecular machines, membrane proteins, viral capsids, fibrils and large molecular assemblies. We show this large panel in order to provide an overview over a range of representative systems under study, rather than a single best performing model system. We discuss both carbon-13 and proton-detected experiments, and show that in C-13 spectra substantially higher numbers of peaks can be resolved compared to 850 MHz while for H-1 spectra the most impressive increase in resolution is observed for aliphatic side-chain resonances.

Publication status

published

Editor

Book title

Volume

75 (6)

Pages / Article No.

255 - 272

Publisher

Springer

Event

Edition / version

Methods

Software

Geographic location

Date collected

Date created

Subject

Solid-state NMR; Magic-angle spinning; Biomolecular NMR; High field; Helicases; Viruses

Organisational unit

03496 - Meier, Beat H. (emeritus) / Meier, Beat H. (emeritus) check_circle
08829 - Ernst, Matthias (Tit.-Prof.) check_circle
09609 - Jonas, Stefanie / Jonas, Stefanie check_circle
03412 - Glockshuber, Rudolf (emeritus) / Glockshuber, Rudolf (emeritus) check_circle

Notes

Funding

741863 - Faster magic-angle spinning leads to a resolution revolution in biological solid-state NMR (EC)
159707 - NMR studies in the Solid State (SNF)
188711 - NMR studies in the Solid State (SNF)

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