New publication:
mr.copernicus.org/articles/7/2...
Congrats to Lea Becker for this work, which she lead from the experiment design to the manuscript. Amazing to work with PhD students like Lea.
We show how to accelerate 19F solid-state #NMR experiments, with application to a 0.5 MDa large protein.
Methodology of our train vs plane CO2 emissions are published in our analysis of conference travel:
mr.copernicus.org/articles/6/2...
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.
I heard many great lectures of yours, and have no doubt that this is highly deserved. Congrats!
Scientists: How long have you waited for journal editors to decide whether the journal sends your manuscript out for review?
I’m at 2+ months with a “prestigious” journal — not easy when working in a competitive field.
What’s the longest you’ve experienced?
#AcademicPublishing #PeerReview
New preprint, a technical paper showing how 19F #NMR of proteins in solids can be accelerated, lead by Lea Becker at @istaresearch.bsky.social.
mr.copernicus.org/preprints/mr...
Magnetic Resonance has an open interactive public peer reviewing system, where anyone can contribute to the discussion.
Very nice preprint that shows that protein crystallographic structures can be used to reveal the entropy of ligand binding.
www.biorxiv.org/content/10.6...
A recent podcast by Stephanie Wankowicz and James @fraserlab.com picked up our work (with Alex Bronstein & coworkers) on Guiding AlphaFold3 with experimental data (cryoEM, X-ray, NMR) to generate protein ensembles. (Thanks for the kind words 🙂)
👉 creators.spotify.com/pod/profile/... (from 35:50)
Ben will talk about his recent work on relaxation-dispersion MAS NMR, including published work )https://pubs.acs.org/doi/full/10.1021/jacs.5c09057 and some new ideas on analysis of relaxation-dispersion NMR to probe microsecond dynamics.
📢 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.
Thanx & congrats @ivasucec.bsky.social Undina Guillerm, Jakob Schneider for a heroic effort. (No doubt: this is the paper with the biggest NMR set from our lab) And Francois Dehez for lots of MD simulations, Nils Wiedemann’s lab for yeast work and Karin Busch’s lab for single-molecule tracking.
🧵8/8
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
Moreover, with lots of methyl-TROSY #NMR spectra — overcoming substantial challenges related to studies of large proteins by NMR — we also resolved, for the first time, how preproteins bind Tom70.
🧵6/8
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
We deciphered Tom22 ’s actual role: its transient helix competes with precursor proteins for binding to the two “real” receptor (Tom20, Tom70). In doing so, Tom22 acts as a precursor-protein displacement element, right above the TOM pore, to release precursor protein for translocation
🧵4/8
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
Almost all mitochondrial proteins are imported through the TOM complex: a beta-barrel pore and “receptor proteins” on the cytosolic side. The “central receptor” protein, Tom22, has remained enigmatic. In cryoEM structures, Tom22 was mostly unresolved, or in contradictory conformations.
🧵2/8
📢 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
📢 Join us at the first Austrian #NMR meeting.
Organised by a fantastic group of young international NMR researchers, this meeting is great opportunity for postdocs and students to contribute their science with a talk or poster. And to see great invited speakers.
austrian-nmr-meeting.pages.ist.ac.at
There are many opportunities in many groups. Check the research on the ISTA web site ista.ac.at
In our group we specifically look for candidates with a strong interest in structural biology and NMR. Experience in protein production, and/or NMR, possibly also in ML and EM, are particularly welcome.
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...
#NMR spectroscopists in and around Austria: join us for this meeting.
A few great keynote speakers, and lots of space for contributed talks from students and postdocs. Taking place at ISTA @istaresearch.bsky.social in February 2026
So excited to announce the first 🧲 Next Austrian NMR Meeting 🧲, happening @ ISTA, Feb 26–27, 2026! Plus a satellite workshop, 💊 “ #NMR in #DrugDiscovery” 🧭 on Feb 25!
📅 Registration: Dec 1, 2025
🌐 Program, venue: austrian-nmr-meeting.pages.ist.ac.at
#NMRchat #Austria 1/4
Wichtig für Klosterneuburg. Und auch für alle am @istaresearch.bsky.social
Bitte hier unterzeichnen: mein.aufstehn.at/petitions/ra...
The course results were not only presented in our Institute Colloquium, but we worked on a detailed analysis of NMR conferences and published the results mr.copernicus.org/articles/6/2...
See also:
ista.ac.at/en/news/carb...
2) Trains do emit much less CO2 than planes per km and person, also when considering all the infrastructure. The savings can be an order of magnitude (and in most cases 3-4x, depending on the travel start/destination)
3) Per-person CO2 emissions to travel to a #EUROMAR #NMR conference is above 1 ton
In brief:
1) yes, carbon emissions due to conference travel are substantial (can be tens of tons of CO2 per year for some colleagues -- >10-fold more than the per-person "budget" to stay within a 2°C warming "goal", which in itself leads already to massive changes to our daily lives.
I had the pleasure to work with amazing students at @istaresearch.bsky.social on a nice "side project": Understanding the travel-related carbon emissions of our institute, and how much planes pollute (compared to trains) -- and then applying all this to analyze the footprint of #NMR conferences.
->🧵
Looking forward to hosting Kresten Lindorff-Larsen's talk tomorrow.
I am looking forward to seeing ISTA's main lecture hall of full, and hearing the latest developments of tools to predict, design and study intrinsically disordered proteins.
@istaresearch.bsky.social
