paulschanda.bsky.social

The ICMRBS conference in Davos has been fantastic. Relaxed atmosphere, top science, great opportunities to connect. I'm happy to be part of the #NMR community, a supportive & friendly crowd. Thanks @icmrbs2026.bsky.social for everything! The (short) bike trip back was a nice way to finish the week.

On my way to @icmrbs2026.bsky.social. From Austria through beautiful Slovenia, and the Dolomites. Looking forward to a nice conference. When I see the terribly dry Alps, I have mixed feelings about these conferences that bring together people from around the world. But clearly, they are useful.

Basically this means that if I take this budget seriously, if I go to the US every year, I exhausted the annual limit within a day. Eating? Heating? Housing? Doing research? Well I may, but not if I take the carbon budget seriously. So where are my priorities? Or do I just not care? Tough choices.

On my way to @icmrbs2026.bsky.social. From Austria through beautiful Slovenia, and the Dolomites. Looking forward to a nice conference. When I see the terribly dry Alps, I have mixed feelings about these conferences that bring together people from around the world. But clearly, they are useful.

With a couple of new impressions (Italy - damn, my Italian is still not quite up to speed- ) I take the liberty to share a few more thoughts about conference travel. 🧵

📢 New publication. We answered an old question in structural biology: (how) does the crystal lattice impact proteins? In particular, how does the crystal restrict the protein's dynamics? We used local probes of dynamics: the rotation of aromatic rings. 🧵 www.nature.com/articles/s41...

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.

📢 New publication. We answered an old question in structural biology: (how) does the crystal lattice impact proteins? In particular, how does the crystal restrict the protein's dynamics? We used local probes of dynamics: the rotation of aromatic rings. 🧵 www.nature.com/articles/s41...

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!

📢 New publication. We answered an old question in structural biology: (how) does the crystal lattice impact proteins? In particular, how does the crystal restrict the protein's dynamics? We used local probes of dynamics: the rotation of aromatic rings. 🧵 www.nature.com/articles/s41...

Returning from an amazing Proteostasis meeting, with lots of new ideas & grateful for great feedback about our mitochondrial-import work. Traveling back from Frankfurt to Vienna by train, I am reminded of the CO2-emissions savings of train vs. plane travel. Also in 2026, I won't take a plane.

📢 Check out Ben Tatman's talk in the Magnetic Resonance Seminar series online (see details below). He will talk about methods to probe protein dynamics by magic-angle spinning #NMR. Friday, Jan 23, noon CET.

📢 New preprint alert! How do proteins enter mitochondria? We uncovered a surprising mechanism at the mitochondrial entry gate—using #NMR, in vivo single-particle tracking, yeast experiments, and MD simulations to crack the code. www.biorxiv.org/content/10.6... #StructuralBiology #Mitochondria 🧵 1/8

Collectively, our data reveal a new functional mechanism, which nature came up with to deal with the contradictory requirements of preprotein binding to the receptors, but also efficient release for translocation. This dynamic mechanism is likely in place at many similar systems. 🧵7/8

📢 New preprint alert! How do proteins enter mitochondria? We uncovered a surprising mechanism at the mitochondrial entry gate—using #NMR, in vivo single-particle tracking, yeast experiments, and MD simulations to crack the code. www.biorxiv.org/content/10.6... #StructuralBiology #Mitochondria 🧵 1/8

These data suggest another role: keeping Tom20 and Tom70 in vicinity of the TOM gate. We used single-molecule tracking experiments in live cells to investigate this role. Indeed: Tom22’s transient helix is a key element that keeps the receptor proteins close to the import gate. 🧵5/8

📢 New preprint alert! How do proteins enter mitochondria? We uncovered a surprising mechanism at the mitochondrial entry gate—using #NMR, in vivo single-particle tracking, yeast experiments, and MD simulations to crack the code. www.biorxiv.org/content/10.6... #StructuralBiology #Mitochondria 🧵 1/8

We found that the cytosolic domain of Tom22— traditionally called a “receptor” — is mostly unfolded, with a short transient helix. MD simulations show the range of states. But how does a receptor interact with the incoming precursor proteins? And is this preprotein-bining even its actual role? 🧵3/8

📢 New preprint alert! How do proteins enter mitochondria? We uncovered a surprising mechanism at the mitochondrial entry gate—using #NMR, in vivo single-particle tracking, yeast experiments, and MD simulations to crack the code. www.biorxiv.org/content/10.6... #StructuralBiology #Mitochondria 🧵 1/8

The PhD call at @istaresearch.bsky.social is open. Get a glimpse on the work of Jakob, a PhD student in our group www.instagram.com/reel/DSjvCo4... Applications: phd.pages.ista.ac.at/phd-applicat...