Publications

Challenges in analyzing NMR Relaxation data

Because the light is better here: correlation-time analysis by NMR.
Angew. Chem. Int. Ed. 2017, 56, 13778-13783.
A. A. Smith, M. Ernst, B. H. Meier
https://doi.org/10.1002/ange.201707316

Model-Free or Not?
Front. Mol. Biosci. 2021, 8, 727553.
K. Zumpfe, A.A. Smith.
https://doi.org/10.3389/fmolb.2021.727553

Theory

Optimized ‘detectors’ for dynamics analysis in solid-state NMR.
J. Chem. Phys. 2018, 148, 045104
A. A. Smith, M. Ernst, B. H. Meier
https://doi.org/10.1063/1.5013316

Reducing bias in the analysis of solution-state NMR data with dynamics detectors.
J. Chem. Phys. 2019, 151, 034102.
A. A. Smith, M. Ernst. B. H. Meier, F. Ferrage.
https://doi.org/10.1063/1.5111081

Interpreting NMR dynamic parameters via the separation of reorientational motion in MD simulation.
J. Magn. Reson. Open, 2022, 10-11, 100045 2022
A. A. Smith
https://doi.org/10.1016/j.jmro.2022.100045

Applications

A method to construct the dynamic landscape of a bio-membrane with experiment and simulation.
Nature Communications. 2022, 13, 108
A. A. Smith, A. Vogel, O. Engberg, P. H. Hildebrand, D. Huster.
https://doi.org/10.1038/s41467-021-27417-y

Experimental characterization of the Hepatitis B virus capsid dynamics by solid-state NMR.
Front. Mol. Biosci. 2022, 8, 807577.
A. A. Malär, M. Callon, A. A. Smith, S. Wang, L. Lecoq, C. Pérez-Segura, J. A. Hadden-Perilla, A. Böckmann, B. H. Meier.
https://doi.org/10.3389/fmolb.2021.807577

How wide is the window opened by high-resolution relaxometry on the internal dynamics of proteins in solution?
J. Biomol. NMR. 2021, 75, 119-131.
A. A. Smith, M. Ernst, B. H. Meier, F. Ferrage.
https://doi.org/10.1007/s10858-021-00361-1

Localized and collective motions in HET-s(218-289) Fibrils from Combined NMR Relaxation and MD Simulation.
Angew. Chem. Int. Ed. 2019, 58, 9383-9388
A. A. Smith, M. Ernst, S. Riniker, B. H. Meier.
https://doi.org/10.1002/anie.201901929