Passionate for integrated structural biology, including NMR and many more. Particularly interested in protein dynamics, and therefore chaperones, enzymes and mitochondrial protein import.
Fortunate to lead a great research team at IST Austria.
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The relevance of this work goes far beyond our favourite pet protein (GB1 here). It has implications for what is becoming very popular these days: protein-dynamics studies by #crystallography, such as with #XFEL sources. Our study shows how dynamics is impacted in the crystal.
It has been a fantastic and fun journey with collaborators across fields and continents: particularly Lea M Becker, the driving force behind the #MAS #NMR, together with Ben Tatman at @istaresearch.bsky.social. Chris Chipot (#MDsimulations) at @cnrs.fr , Sylvain Engilberge at @esrf.fr .
We combined NMR spectroscopy in solution and in crystals, and crystallography (including at room temperature), and MD simulations.
Our key finding: aromatic ring flips are massively slowed down by the crystal. More than 1000x slower than in solution!
Aromatic rings can rotate by 180° -- so-called ring flips -- but to do so their surrounding needs to make some space. These collective dynamic modes are sometimes called "breathing motions", a poorly defined term that has been around for 45 years. But what is this? And does it exist in crystals?
MD simulations told us about the underlying mechanisms. And also show that what is called "breathing motion" is actually a complex rearrangement of interactions that have to be re-shuffled such that the ring can rotate. T-dependent MAS NMR told us how the crystal restricts such motions.
