To find an updated list of all papers, best check:
Here are a few papers we are particularly excited about:
Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes
bioRxiv. 2025
We address a long-standing question in structural biology: (how) does the crystalline environment alter the behavior of proteins? By combining MAS NMR, specific isotope labeling, crystallography and enhanced-sampling MD simulations, we find that aromatic ring flips — a hallmark of collective motions in proteins — are slowed down by several orders of magnitude in crystals compared to solution. Our work has important implications for crystallography, including XFEL studies of protein dynamics.
Bumps on the Road: The Way to Clean Relaxation Dispersion Magic-Angle Spinning NMR
J. Am. Chem. Soc. 2025, 147, 32, 29315–29326 https://pubs.acs.org/doi/full/10.1021/jacs.5c09057
This study goes quite a bit into MAS NMR theory to figure out how to improve experiments that probe microsecond dynamics. Our improved method is able to deliver information about such motions – which often are functionally important – much faster and with higher precision than previously available methods.
Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR
Nat. Commun. 13: 1927, https://www.nature.com/articles/s41467-022-29423-0
Sometimes the “invisible” is the most important part. In this large oligomeric enzyme, a loop that crystallography and EM can hardly see, turns out to be a key functional element within the large catalytic chamber. Using MAS NMR, we quantify its motion and provide evidence for its role in stabilizing substrate in the active site.
Structural basis of client specificity in mitochondrial membrane-protein chaperones
Science Advances, 6, 51: eabd0263, https://advances.sciencemag.org/content/6/51/eabd0263
Chaperones are generally thought to bind their client proteins promiscuously by hydrophobic interactions, but this raises the question how chaperones achieve client specificity. Combining solution-NMR, SAXS, MD simulations and biochemistry, we show that the membrane-protein chaperones TIM9·10 and TIM8·13 achieve specificity by differentially employing both hydrophobic and hydrophilic interactions. We thus clarify the role of chaperoning in the mitochondrial intermembrane-space, and more generally open new ways of thinking of chaperone function.
Mechanism of the allosteric activation of the ClpP protease machinery by active-site inhibitors
Science Advances, 5 (9), eaaw3818 https://advances.sciencemag.org/content/5/9/eaaw3818
The 300 kDa-large ClpP has a stunning property: as our study reveals, sub-stoichiometric amounts of an inhibitor activates the enzymatic activity. How can an inhibitor activate an enzyme? Using a multi-technique approach—including solution-state and solid-state NMR—we unraveled the allosteric mechanism driving this activation.
Aromatic ring dynamics and excited states detected in a half-megadalton aminopeptidase by specific labeling and MAS NMR
J. Am. Chem. Soc., 141 (28), 11183–11195 https://pubs.acs.org/doi/10.1021/jacs.9b04219
Paper highlighted in ‘Faculty of 1000’: https://f1000.com/prime/735988056#eval793563211
In this study, we develop combined isotope-labeling/MAS NMR techniques to gain unprecedented insight into the dynamics of phenylalanines, and apply the methodology to a 0.5 MDa-large protein complex. We reveal microsecond time scale dynamics in the entry pore to the catalytic chamber. Moreover, we investigated how ring flips are activated, by studying dynamics over a large temperature range down to 100 K.