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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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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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