@article{20258,
  abstract     = {The specific introduction of ^1H-^13C or ^1H-^15N moieties into otherwise deuterated proteins holds great potential for high-resolution solution and magic-angle spinning (MAS) NMR studies of protein structure and dynamics. Arginine residues play key roles for example at active sites of enzymes. Taking advantage of a chemically synthesized Arg with a ^13C-^1H2 group in an otherwise deuterated backbone, we demonstrate here the usefulness of proton-detected MAS NMR approaches to probe arginine dynamics. In experiments with crystalline ubiquitin and the 134 kDa tetrameric enzyme malate dehydrogenase we detected a wide range of motions, from sites that are rigid on time scales of at least tens of milliseconds to residues undergoing predominantly nanosecond motions. Spin-relaxation and dipolar-coupling measurements enabled quantitative determination of these dynamics. We observed microsecond dynamics of residue Arg54 in crystalline ubiquitin, whose backbone is known to sample different β-turn conformations on this time scale. The labeling scheme and experiments presented here expand the toolkit for high-resolution proton-detected MAS NMR.},
  author       = {Rohden, Darja and Napoli, Federico and Kapitonova, Anna and Tatman, Benjamin and Lichtenecker, Roman J. and Schanda, Paul},
  issn         = {1089-8638},
  journal      = {Journal of Molecular Biology},
  number       = {23},
  publisher    = {Elsevier},
  title        = {{Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme}},
  doi          = {10.1016/j.jmb.2025.169379},
  volume       = {437},
  year         = {2025},
}

@article{20321,
  abstract     = {Microsecond-to-millisecond motions are instrumental for many biomolecular functions, including enzymatic activity and ligand binding. Bloch-McConnell Relaxation Dispersion (BMRD) Nuclear Magnetic Resonance (NMR) spectroscopy is a key technique for studying these dynamic processes. While BMRD experiments are routinely used to probe protein motions in solution, the experiment is more demanding in the solid state, where dipolar couplings complicate the spin dynamics. It is believed that high deuteration levels are required and sufficient to obtain accurate and quantitative data. Here we show that even under fast magic-angle spinning and high levels of deuteration artifactual “bumps” in 15N R1ρ BMRD profiles are common. The origin of these artifacts is identified as a second-order three-spin Mixed Rotational and Rotary Resonance (MIRROR) recoupling condition. These artifacts are found to be a significant confounding factor for the accurate quantification of microsecond protein dynamics using BMRD in the solid state. We show that the application of low-power continuous wave (CW) decoupling simultaneously with the 15N spin-lock leads to the suppression of these conditions and enables quantitative measurements of microsecond exchange in the solid state. Remarkably, the application of decoupling allows the measurement of accurate BMRD even in fully protonated proteins at 100 kHz MAS, thus extending the scope of μs dynamics measurements in MAS NMR.},
  author       = {Tatman, Benjamin and Sridharan, Vidhyalakshmi and Uttarkabat, Motilal and Jaroniec, Christopher P. and Ernst, Matthias and Rovo, Petra and Schanda, Paul},
  issn         = {1520-5126},
  journal      = {Journal of the American Chemical Society},
  number       = {32},
  pages        = {29315--29326},
  publisher    = {American Chemical Society},
  title        = {{Bumps on the road: The way to clean relaxation dispersion magic-angle spinning NMR}},
  doi          = {10.1021/jacs.5c09057},
  volume       = {147},
  year         = {2025},
}

@misc{19696,
  author       = {Tatman, Benjamin},
  publisher    = {Institute of Science and Technology Austria},
  title        = {{Dataset for "Bumps on the Road: The Way to Clean Relaxation Dispersion in the Solid State"}},
  doi          = {10.15479/AT-ISTA-19696},
  year         = {2025},
}