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.

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.
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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.
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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.
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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.
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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
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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?
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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.

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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 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.

here is the correct link: ista.ac.at/en/job/tenur...

Preprint
www.biorxiv.org/content/10.1...

Data
doi.org/10.7910/DVN/...

Code
github.com/sai-advaith/...

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