Probing the energy landscape of α-Synuclein amyloid fibril formation by systematic K-to-Q mutagenesis https://www.biorxiv.org/content/10.1101/2025.11.01.685997v1

In the nucleus, many intrinsically disordered proteins (IDPs) form condensates. What IDP sequence features drive this behavior? We developed CondenSeq, a high-throughput approach to measure nuclear condensate formation, and applied it to ~14,000 IDPs to find out! rdcu.be/eq975

In collaboration with the @lindorfflarsen.bsky.social group we release our map of degrons in >5,000 human cytosolic proteins with >99% coverage. A machine learning model trained on the data identifies missense variants forming degrons in exposed & disordered regions. Work led by @vvouts.bsky.social.

mRNA display continues to astound. Fantastic collaboration with Alex Buell, led by the peerless @rasmusnorrild.bsky.social. ~100,000 peptides and their propensity to join the phase separation of a model disordered protein. doi.org/10.1101/2024...

We are finally ready to share the preprint version about our use of mRNA-display to study what makes disordered proteins form condensates, at the proteome-scale! Check it out here:

Thermodynamic Stability Modulates Chaperone-Mediated Disaggregation of α-Synuclein Fibrils https://www.biorxiv.org/content/10.1101/2024.12.19.629136v1

Check out @rasmusnorrild.bsky.social's work with Alex Buell and Joe Rogers developing and using Condensate Partitioning by mRNA-Display to probe phase separation of ~100.000 sequences, and @sobuelow.bsky.social's simulations to support and analyse the experiments www.biorxiv.org/content/10.1...

We are finally ready to share the preprint version about our use of mRNA-display to study what makes disordered proteins form condensates, at the proteome-scale! Check it out here:

Proteome-scale quantification of the interactions driving condensate formation of intrinsically disordered proteins https://www.biorxiv.org/content/10.1101/2024.12.21.629870v1