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DTSTART;TZID=Europe/Paris:20251014T170000
DTEND;TZID=Europe/Paris:20251014T180000
DTSTAMP:20260522T193102
CREATED:20250829T072016Z
LAST-MODIFIED:20251008T122724Z
UID:1647-1760461200-1760464800@www.globalnmr.org
SUMMARY:Andreas Meyer
DESCRIPTION:Using 19F to Study Paramagnetic Biomolecules at the Nanoscale with Electron Nuclear Double Resonance \n19F labels are well established in NMR spectroscopy and allow accessing specific molecular information within biomolecular frameworks such as proteins. In case of radical enzymes or paramagnetic metalloproteins\, the molecular structure around the paramagnetic center within a radius of up to ca. 20 Å can be investigated by electron nuclear double resonance (ENDOR) spectroscopy\, benefitting from the high electron spin polarization. The method can also be applied to diamagnetic molecules if paramagnetic spin labels are used.In this talk\, the basic principles of 19F ENDOR will be presented in an instructive fashion\, followed by an overview of how the method developed in the past five years. As an application\, the use of 19F ENDOR in studying the proton coupled electron transfer of ribonucleotide reductase\, a tetrameric radical enzyme with more than 2200 residues\, will be showcased. \n8:00 AM California or 11:00 AM Boston or 5:00 PM Paris or 8:30 PM Delhi
URL:https://www.globalnmr.org/upcoming-discussions/andreas-meyer/
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DTSTART;TZID=Europe/Paris:20251021T170000
DTEND;TZID=Europe/Paris:20251021T180000
DTSTAMP:20260522T193102
CREATED:20250829T072044Z
LAST-MODIFIED:20251008T122331Z
UID:1649-1761066000-1761069600@www.globalnmr.org
SUMMARY:Mikael Akke
DESCRIPTION:Resolving Protein–Ligand Binding Pathways by NMR Relaxation: Conformational Selection vs Induced Fit \nProtein–ligand binding is essential for biological function. A long-standing question is whether ligand binding occurs via conformational selection (CS) or induced fit (IF). Using relaxation dispersion experiments with varying ligand concentration\, we measured the 4-state binding kinetics encompassing both the CS and IF pathways in galectin-3. We determined the ligand affinity of each pathway\, all rate constants and populations\, and the relative flux through each pathway — all of which provide a very rich understanding of protein–ligand binding and some surprising results. \n8:00 AM California or 11:00 AM Boston or 5:00 PM Paris or 8:30 PM Delhi
URL:https://www.globalnmr.org/upcoming-discussions/mikael-akke/
ATTACH;FMTTYPE=image/jpeg:https://www.globalnmr.org/wp-content/uploads/2025/08/MikaelAkke.jpg
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DTSTART;TZID=Europe/Paris:20251028T170000
DTEND;TZID=Europe/Paris:20251028T180000
DTSTAMP:20260522T193102
CREATED:20250829T071909Z
LAST-MODIFIED:20251008T122220Z
UID:1643-1761670800-1761674400@www.globalnmr.org
SUMMARY:Raphaële Clément
DESCRIPTION:Advancing Magnetic (Resonance) Methods to Track Processes inParamagnetic Battery Electrodes \nSolid-state NMR has become an indispensable tool for quantifying defects and tracking the nature and reversibility of local structure changes in battery electrode materials during charge and discharge. Yet\, probing paramagnetically concentrated systems with NMR remains extremely challenging. Achieving sufficient spectral resolution requires low magnetic fields and ultrafast spinning—conditions that are currently incompatible with real-time operando studies. At the same time\, improved theoretical methodologies for predicting paramagnetic NMR shifts are needed to unravel the complexity of spectra acquired at different stages of cycling.In this talk\, I will first present our development of operando magnetometry and EPR approaches that complement high-resolution ex situ solid-state NMR\, offering new insights into the interplay between cation disorder and redox processes in LixNi1-yMnyO2 cathodes.1\,2 In the second part\, I will introduce an ab initio cluster expansion Monte Carlo framework for computing finite-temperature Fermi contact shifts with significantly improved accuracy compared to methods to date.3\,4 Together\, these developments move us closer to fully exploiting magnetic resonance for tracking battery processes in action.[1] Nguyen\, H.\, Bassey\, E.\, Foley\, E.\, Kitchaev\, D.\, Giovine\, R.\, Clément\, R.\, J. Magn. Reson.\, 2024\, 368\, 107772.[2] Nguyen\, H.\, Zaveri\, A.\, Cui\, W.\, Silverstein\, R.\, Kurzhals\, P.\, Sicolo\, S.\, Bianchini\, M.\, Seidel\, K.\, Clément\, R.\, 2023\, Adv. Funct. Mater.\, 2306168.[3] Garcia Ponte\, G.\, Behara\, S.\, Bassey\, E.\, Clément\, R.\, Van der Ven\, A.\, Chem. Mater. 2025\, 37\, 5\, 1835–1846.[4] Bassey\, E.\, Sebti\, E.\, Van der Ven\, A.\, Clément\, R.\, in preparation. \n8:00 AM California or 11:00 AM Boston or 5:00 PM Paris or 8:30 PM Delhi
URL:https://www.globalnmr.org/upcoming-discussions/raphaele-clement/
ATTACH;FMTTYPE=image/jpeg:https://www.globalnmr.org/wp-content/uploads/2025/08/Raphaele.jpeg
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