Impact of magnetic field strength on resolution and sensitivity of proton resonances in biological solids.
J. Phys. Chem. C. 124, 22631-22637 (2020)
Sensitivity and resolution together determine the quality of NMR spectra in biological solids. Higher magic angle spinning frequencies yield a more efficient suppression of the coupling network and enable atomic-level investigations of protonated protein samples. On the other hand, truncation effects induced by higher magnetic fields have an impact on the achievable sensitivity and resolution. In this work, we address the question of how the proton dipolar coupling network affects the magnetic field strength-dependent gains in sensitivity and resolution. We find that-beyond the canonical B-0(3/2) dependence-an additional factor of 2 in sensitivity can be achieved for residues embedded in the core of the protein, when the static magnetic field induces a transition from the strong- to the weak-coupling limit. The experiments are carried out using a selectively methyl-protonated ((13)CH3) alpha-spectrin SH3 sample, at magnetic field strengths of 11.75 T (H-1 Larmor frequency of 500 MHz) and 23.5 T (H-1 Larmor frequency of 1 GHz).
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Publication type
Article: Journal article
Document type
Scientific Article
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Keywords
State Nmr-spectroscopy; 100 Khz; Proteins; Simulation; H-1
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Language
english
Publication Year
2020
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2020
ISSN (print) / ISBN
1932-7447
e-ISSN
1932-7455
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Volume: 124,
Issue: 41,
Pages: 22631-22637
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American Chemical Society (ACS)
Publishing Place
Washington, DC
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Peer reviewed
POF-Topic(s)
30203 - Molecular Targets and Therapies
Research field(s)
Enabling and Novel Technologies
PSP Element(s)
G-503090-001
Grants
project "e-Infrastruktura CZ" (e-INFRA) within the program Projects of Large Research, Development and Innovations Infrastructures
EU access project iNext
European Research Council (ERC)
Czech Science Foundation
CNRS
Center for Integrated Protein Science Munich (CIPS-M)
Deutsche Forschungsgemeinschaft (DFG)
Helmholtz-Gemeinschaft
German Research Foundation, DFG
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Erfassungsdatum
2020-12-08