Rasmus Krogh Norrild
@rasmusnorrild.bsky.social
📤 275
📥 188
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Postdoc with Alexander Büll at DTU. Interested in all things protein, biochemistry, and biophysics.
reposted by
Rasmus Krogh Norrild
bioRxiv Biophysics
13 days ago
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
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Rasmus Krogh Norrild
Kalli Kappel
5 months ago
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
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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...
https://rdcu.be/eq975
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reposted by
Rasmus Krogh Norrild
Rasmus Hartmann-Petersen
6 months ago
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
.
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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...
https://www.biorxiv.org/content/10.1101/2025.05.10.653233v1
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reposted by
Rasmus Krogh Norrild
Joe Rogers
10 months ago
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...
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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 ...
https://doi.org/10.1101/2024.12.21.629870
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reposted by
Rasmus Krogh Norrild
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:
add a skeleton here at some point
11 months ago
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reposted by
Rasmus Krogh Norrild
bioRxiv Biophysics
11 months ago
Thermodynamic Stability Modulates Chaperone-Mediated Disaggregation of α-Synuclein Fibrils
https://www.biorxiv.org/content/10.1101/2024.12.19.629136v1
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reposted by
Rasmus Krogh Norrild
Kresten Lindorff-Larsen
11 months ago
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...
add a skeleton here at some point
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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:
add a skeleton here at some point
11 months ago
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6
reposted by
Rasmus Krogh Norrild
bioRxiv Biophysics
11 months ago
Proteome-scale quantification of the interactions driving condensate formation of intrinsically disordered proteins
https://www.biorxiv.org/content/10.1101/2024.12.21.629870v1
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