Rasmus Krogh Norrild

Characterizing protein sequence determinants of nuclear condensates by high-throughput pooled imaging with CondenSeq Nature Methods - CondenSeq is an imaging-based, high-throughput platform for characterizing condensate formation within the nuclear environment, uncovering the protein sequence features that...

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

A complete map of human cytosolic degrons and their relevance for disease Degrons are short protein segments that target proteins for degradation via the ubiquitin-proteasome system and thus ensure timely removal of signaling proteins and clearance of misfolded proteins fro...

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.

Proteome-scale quantification of the interactions driving condensate formation of intrinsically disordered proteins The formation of biomolecular condensates is involved in compartmentalisation, regulation, and signalling across most living organisms. Condensation can be driven by phase separation of proteins, and ...

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:

I am not quite sure that I can follow your question. We are indeed surprised that partitioning to DDX4N1 condensates appear to generalise to the behaviour of unrelated IDRs, so it most be sufficiently "promiscuous". Here, interactions seem to be better explained by partitioning rather than binding.

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

We also had the discussion a while back, and also ended up with the "signal above baseline" from laser scattering. Something like signal beyond 10 standard deviations of noise. But it does not help that you get "nano-cluster", or what else you call it, before full phase separation.