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Xue, K. ; Sarkar, R. ; Lalli, D.* ; Koch, B.* ; Pintacuda, G.* ; Tosner, Z.* ; Reif, B.

Impact of magnetic field strength on resolution and sensitivity of proton resonances in biological solids.

J. Phys. Chem. C. 124, 22631-22637 (2020)
Verlagsversion Forschungsdaten DOI
Open Access Green: Postprint online verfügbar 12/2021
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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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter State Nmr-spectroscopy; 100 Khz; Proteins; Simulation; H-1
ISSN (print) / ISBN 1932-7447
e-ISSN 1932-7455
Quellenangaben Band: 124, Heft: 41, Seiten: 22631-22637 Artikelnummer: , Supplement: ,
Verlag Royal Society of Chemistry (RSC)
Verlagsort Washington, DC
Begutachtungsstatus Peer reviewed
Förderungen 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