Impact of Magnetic Field Strength on Resolution and Sensitivity of Proton Resonances in Biological Solids

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F20%3A10420997" target="_blank" >RIV/00216208:11310/20:10420997 - isvavai.cz</a>
Result on the web
<a href="https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=UN6Cx5Fe2o" target="_blank" >https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=UN6Cx5Fe2o</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/acs.jpcc.0c05407" target="_blank" >10.1021/acs.jpcc.0c05407</a>

Result language
angličtina
Original language name
Impact of Magnetic Field Strength on Resolution and Sensitivity of Proton Resonances in Biological Solids
Original language description
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).
Czech name
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Czech description
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Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
—
OECD FORD branch
10403 - Physical chemistry

Project
<a href="/en/project/GC20-00166J" target="_blank" >GC20-00166J: Development of Optimal Control derived experiments for biological MAS solid-state NMR</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2020
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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