georghochberg
Evolutionary biochemist and protein complex enthusiast at the University of Marburg.
- A new preprint from the lab. I won't do a tweetorial until this is peer reviewed, but I think it's a banger, led by @JedNzy. It's about Rubisco and what chaperones are really for. He's on the market, get him while you can. www.biorxiv.org/content/10.1...
- The Beeby lab's magnum opus on the Campylobacter flagellum is out. This is a uniquely powerful flagellum and how it evolved out of simpler precursors will keep us busy for a while still. Check it out! www.nature.com/articles/s41...
- Franziska did a spectacularly successful PhD in my group and to a large extend set up the lab when we first started. I'm extremely happy for her (though not the least bit surprised) that she won these very important awards for her PhD. Watch this one, great things are certain to come.
- 📢 Congratulations 𝗗𝗿. 𝗙𝗿𝗮𝗻𝘇𝗶𝘀𝗸𝗮 𝗦𝗲𝗻𝗱𝗸𝗲𝗿 for receiving the Otto Hahn Medal and Otto Hahn Award from @maxplanck.de ! 🎉 The honors recognize her exceptional work @georghochberg.bsky.social. 🌟 Exciting times ahead! #MaxPlanck #ResearchExcellence www.mpi-marburg.mpg.de/1511259/2025...
- New paper from the lab from Sriram Garg in my group. We introduce a general substitution matrix for structural phylogenetics. I think this is a big deal, so read on below if you think deep history is important. academic.oup.com/mbe/advance-...
- Deep phylogenetics is important. What genes did LUCA have? Where do eukaryotes come from? How did the major metabolic pathways evolve? All questions whose answers depend on phylogenetic trees that cover vast time-scales.
- Such trees are hard to infer for many reasons. But one big problem is that protein sequences sometimes have just accumulated too many changes to still contain enough information to resolve the things we care about.
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View full threadOh and Sriram should be a co-corresponding author on this with me, but the journal messed this up after the proofs. I hope this will be corrected when the final version is out. He really drove this project.
- An enormous amount of work went into this from so many people: our leadership at the MPI and the university, the scientific team, the administrative support and of course all the scientists that did the science that laid the foundation for all this. What a rush to be part of this!
- 📢 We are proud and delighted that our Microbes for Climate (M4C) Cluster of Excellence has been selected for the 2025 Excellence Strategy! 🌟Together with @unimarburg.bsky.social, we look forward to exciting #microbe research – stay tuned! @unimarburg.bsky.social @maxplanck.de @synmikro.bsky.social
- Dennis from the group contributed to this paper, showing that an assembly chaperone of PSII has identifiable precursors in non-photosynthetic organisms.
- This is a wild paper. The anaerobic biochemistry is definitely worth your while (and beyond me to explain), but let me try to explain why this is also an evolutionary bombshell. This is about how nitrogen fixation evolved as we know it.
- I'm truly excited to announce our new publication in @nature.com unraveling a central picture of the Methyl-coenzyme M reductase (MCR) activation machinery and it's strong ATP dependency - kudos to @rnfr2d2.bsky.social for the fantastic illustration! LINK: www.nature.com/articles/s41...
- Nitrogen fixation is carried out by Nitrogenases. This is the only known enzyme that can break the triple bond of nitrogen. It's essential for life as we know it. They have a special metal cofactor, called the M Cluster, which does this chemistry.
- It's life's most complex metal cofactor, and is part what is known as the Great Clusters - important cofactors that do the redox chemistry that underpins life. Until now, it was known only in nitrogenases and its origins therefore closely tied to the origins of nitrogen fixation.
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View full threadSo congratulations to Fidel, Sophian, Anuj and the rest of the team. I count myself very lucky to have been allowed to be a part of this.
- Now also on here to very occasionally post protein evolution stuff.