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Rasmus Krogh Norrild @rasmusnorrild.bsky.social · 14/10/2026

I wrote a short piece for the Tools of the Trade series in Nature Reviews Molecular Cell Biology breaking down our newly published method, Condensate Partitioning by mRNA-display (CPmD): www.nature.com/articles/s41... Check out the original paper here: www.nature.com/articles/s41...

nature.com

Scaling up measurements of the interactions that build condensates - Nature Reviews Molecular Cell Biology

Condensate partitioning by mRNA-display (CPmD) enables high-throughput assessment of protein (domain) propensity for condensate formation.

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Reposted by Rasmus Krogh Norrild

bioRxiv Biophysics @biorxiv-biophys.bsky.social · 03/11/2025

Probing the energy landscape of α-Synuclein amyloid fibril formation by systematic K-to-Q mutagenesis www.biorxiv.org/content/10.1101/202…

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Reposted by Rasmus Krogh Norrild

Kalli Kappel @kallikappel.bsky.social · 17/06/2025

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

rdcu.be

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...

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Reposted by Rasmus Krogh Norrild

Rasmus Hartmann-Petersen @rhp-lab.bsky.social · 15/05/2025

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.

biorxiv.org

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...

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Reposted by Rasmus Krogh Norrild

Rasmus Krogh Norrild @rasmusnorrild.bsky.social · 21/12/2024

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:

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Rasmus Krogh Norrild @rasmusnorrild.bsky.social · 22/12/2024

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.

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Reposted by Rasmus Krogh Norrild

bioRxiv Biophysics @biorxiv-biophys.bsky.social · 21/12/2024

Thermodynamic Stability Modulates Chaperone-Mediated Disaggregation of α-Synuclein Fibrils www.biorxiv.org/content/10.1101/202…

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Reposted by Rasmus Krogh Norrild

Kresten Lindorff-Larsen @lindorfflarsen.bsky.social · 21/12/2024

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...

Figure 1a from the paper that outlines the method. Caption: "Peptides from the N-terminal IDR of DDX4 were encoded in a DNA library for mRNA display and transcribed using purified T7 RNA polymerase. The resulting mRNA contains a ribosomal binding site (RBS), a coding sequence (CDS) for peptide of interest, and a HA-tag for purification via the translated peptide. The synthetic mRNA (pink) is ligated to a puromycin-containing PEG-linker (black) containing a DNA sequence (blue) that forms a hetero duplex with the mRNA to facilitate single stranded RNA ligation. The resulting mRNA display molecule is purified using the HA-tag and added to an excess of DDX4N1 to measure partitioning of all library members through RNA/DNA sequencing. "

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Rasmus Krogh Norrild @rasmusnorrild.bsky.social · 21/12/2024

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:

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Reposted by Rasmus Krogh Norrild

bioRxiv Biophysics @biorxiv-biophys.bsky.social · 21/12/2024

Proteome-scale quantification of the interactions driving condensate formation of intrinsically disordered proteins www.biorxiv.org/content/10.1101/202…

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Rasmus Krogh Norrild @rasmusnorrild.bsky.social · 05/12/2024

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.

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