Utrecht University
Weingarth Lab
Biomedical Solid-State NMR
We use advanced solid-state NMR methods to study medically important biomolecules and biomaterials at the atomic level and directly in native cellular conditions. Our main research interests are:
Selected Recent Publications
1. Jekhmane, S., Medeiros-Silva, J., Li, J., Kümmerer, F., Müller-Hermes, C., Baldus, M., Roux, B., Weingarth., M., (2019) Nature Comm., 10, 12, Shifts in the selectivity filter dynamics cause modal gating in K+ channels See also Press release
2. Jekhmane, S., Prachar, M., J., Pugliese, R., Fontana, F., Medeiros-Silva, Gelain, F., Weingarth, M., (2019) Angewandte Chemie, in press, Design parameters of tissue engineering scaffolds at atomic scale
3. Medeiros-Silva, J., Jekhmane, S., Paioni, A., Gawarecka, K., Baldus, M., Swiezewska, E., Breukink, E., Weingarth, M., (2018) Nature Comm., 9, 3963, High-resolution NMR studies of antibiotics in cell membranes See here for the Press release & coverage & coverage
4. Visscher, K.M., Medeiros-Silva, J. Mance, D., Rodrigues, J.P.G.L.M., Daniëls, M., Bonvin, A.M.J.J., Baldus, M., Weingarth, M., (2017) Angew. Chem., 56, 13222, Supramolecular organization and functional implications of K+ channel clusters in membranes Selected as Frontispiece
Shehrazade Jekhmane & João Medeiros-Silva et al., Nature Communications (2019) 10, 12, p. 1-11
Shifts in the selectivity filter dynamics cause modal gating in K+ channels
This work provides a
long-needed quantitative description of the selectivity filter dynamics in a
native environment, which is of fundamental importance to understand ion channel function
João Medeiros-Silva et al.,
Nature Communications (2018)
9, 3963, p. 1-10
High-resolution NMR studies of antibiotics in cellular membranes
A powerful NMR approach (integrating proton-detection and 800 MHz DNP) to study promising membrane-active antimicrobial peptides at high-resolution and directly in cellular conditions.
Angewandte Chem. (2017)
56, 13222-13227
A DNP-ssNMR approach to study membrane protein - membrane protein interactions in relation to function in a FRET-like manner
