Ernst Schmid

@ernstschmid.bsky.social

Full stack developer who occasionally wears a lab coat. Currently a machine learning researcher at Manifold Bio.

AlphaFold2-WebGPU now supports AlphaFold-Multimer. As in ColabFold, simply use : to separate chains in the sequence input. It is also becoming much more stable: I was able to predict a 491-aa protein in ~4 minutes in M4 Pro. Chrome currently performs better than Firefox for WebGPU, unfortunately.

Martin Steinegger 🇺🇦@martinsteinegger.bsky.social · 2mo ago

Run AlphaFold2 locally in your browser via WebGPU, no installation needed, it's just a static webpage using your own GPU or CPU. Short proteins run in seconds. Larger ones are still slow: a 291-aa protein takes ~7 minutes on my M4 Pro. ❗It's just a PoC. 🌐 martin-steinegger.github.io/alphafold2-w...

🧬 How is MCM2-7 switched on? Our paper shows DDK phosphorylation exposes Sld3-binding sites on Mcm4/Mcm6. Sld3-Cdc45 then delivers Cdc45 to Mcm2/Mcm5, driving CMG assembly. In summary, our work explains why MCM2-7 phosphorylation is needed to turn on replication. www.nature.com/articles/s41...

Structural insights into Sld3-Sld7-dependent Cdc45 loading during replication initiation - Nature Communications

DNA replication depends on loading Cdc45 onto the MCM2-7 helicase to start DNA unwinding. Here, the authors use cryo-EM to show how phosphorylation enables Sld3-Sld7 to bind MCM2-7 and position Cdc45 ...

nature.com

Most PDB structures report one set of coordinates. But the experimental data behind them, in both X-ray crystallography and cryo-EM, is produced by an ensemble of structures. How to extract this ensemble data at scale has been a quest in structural biology for 40+ years.

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Five years ago, the #AlphaFold Database, a collaboration with Google DeepMind, made predicted protein structures free for everyone to use. Today, the database contains over 260 million structure predictions and is used by more than 3.5 million researchers in 190 countries around the world.

Another chapter of my thesis is out! We asked whether we could pair proteome-wide AlphaFold screening with Tn-seq to identify biologically relevant protein-protein interactions. We identify ClcR (formerly YerH) as a component of the Rod complex in Gram-positive bacteria. www.pnas.org/doi/10.1073/...

A broadly conserved gram-positive lipoprotein regulates cell elongation | PNAS

The cell wall peptidoglycan (PG) protects virtually all bacteria from osmotic lysis and specifies cell shape. Synthesis of this exoskeleton is carr...

pnas.org

My latest work! We found that the autoproteolytic GAIN domain which mediates force responsive signaling in adhesion GPCRs is not unique to eukaryotes. The microbial counterparts anchor diverse adhesion, enzymatic, and toxin domains to the cell surface, enabling release by likely mechanical stimuli.

bioRxiv Microbiology@biorxiv-microbiol.bsky.social · 6mo ago

Microbial GAIN domains undergo autoproteolysis and enable release of diverse cell surface associated proteins https://www.biorxiv.org/content/10.64898/2026.05.12.724683v1

If you use Boltz1/2, BioEmu, Chai1, or other MSA-dependent models, you’re likely using our ColabFold server. Please be considerate! Avoid large submissions across many IPs instead generate the MSA locally. Our server is an old-timer from 2014 and can’t handle that load.

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Unexpectedly, @jurgjn.bsky.social found that running Alphafold3 predictions for protein interactions can yield ipTM scores that are more predictive of true interactions when run in pools of proteins instead of pairwise predictions. Presumably, this reflects some sort of "competition effect".

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