Julian Streit
julianstreit.bsky.social
Julian Streit
@julianstreit.bsky.social
Postdoctoral researcher in computational structural biology at the University of Copenhagen with Kresten Lindorff-Larsen
Reposted by Julian Streit
Our story on GroEL/ES action during cotranslational folding is now published @natcomms.nature.com. Led by former-student Alzbeta Roeselova, and in collaboration with Rado Enchev's lab @crick.ac.uk.
www.nature.com/articles/s41...
GroEL/ES chaperonin unfolds then encapsulates a nascent protein on the ribosome - Nature Communications
The GroEL/ES chaperonin can act during protein synthesis to promote folding. Here, Roeselová et al. show how GroEL captures, remodels and sequesters nascent proteins in its central chamber, while they...
www.nature.com
November 14, 2025 at 1:49 PM
Reposted by Julian Streit
My first full contribution from my time in @opig.stats.ox.ac.uk is now out! Together with @fspoendlin.bsky.social (and with contributions from King Ifashe), we created FlAbDab and FTCRDab: two large-scale, open molecular dynamics datasets to study flexibility in immune receptors.
November 12, 2025 at 9:21 PM
Reposted by Julian Streit
Our work developing a maximum entropy reweighting method to refine all-atom ensembles of IDPs with extensive NMR and SAXS datasets is now out in @natcomms.nature.com:

rdcu.be/eKlK7

Led by @dartmouthchem.bsky.social graduate student Kaushilk Borthakur in collaboration with @bonomimax.bsky.social
Determining accurate conformational ensembles of intrinsically disordered proteins at atomic resolution
Nature Communications - This study demonstrates how to combine molecular dynamics computer simulations with experimental biophysical data to determine accurate atomic-resolution ensembles of...
rdcu.be
October 10, 2025 at 3:33 PM
Reposted by Julian Streit
I'm hiring for a PhD position at Malmö University, Sweden!

The project will focus on molecular modelling of proteins, lipids, and biomolecular condensates at cell membranes.

More details and application form: tinyurl.com/4zm92365

Please feel free to share!

@vetenskapsradet.bsky.social | @mau.se
October 2, 2025 at 7:46 AM
Reposted by Julian Streit
So excited that our lab's first home-grown paper is now available on ChemRxiv!

Kinetic NMR screening: rapidly quantifying fast ligand dissociation in fragment mixtures using ¹⁹F relaxation dispersion | doi.org/10.26434/che... 🧲🧪
Kinetic NMR screening: rapidly quantifying fast ligand dissociation in fragment mixtures using ¹⁹F relaxation dispersion
Ligand-observed NMR is a key tool for detecting weak protein-ligand interactions, but translating binding signals into meaningful affinity measurements remains difficult, limiting the ability to rank ...
doi.org
September 24, 2025 at 12:54 PM
Reposted by Julian Streit
Excited to see our review now on arXiv, written together with @fpesce.bsky.social and @lindorfflarsen.bsky.social

doi.org/10.48550/arX...
New review on computational design of intrinsically disordered proteins 🖥️🍝 by @giuliotesei.bsky.social @fpesce.bsky.social & 👴

doi.org/10.48550/arX...
September 18, 2025 at 9:44 PM
Reposted by Julian Streit
Our paper on:

A coarse-grained model for simulations of phosphorylated disordered proteins

(aka parameters for phospho-serine and -threonine for CALVADOS)

is now published in Biophysical Journal

authors.elsevier.com/a/1lTcE1SPTB...

@asrauh.bsky.social @giuliotesei.bsky.social & Gustav Hedemark
July 22, 2025 at 5:58 AM
New preprint with Benjamin Lang, Richard Kriwacki, John Christodoulou, and M. Madan Babu!
www.biorxiv.org/content/10.1...

Protein Dynamics at Different Timescales Unlock Access to Hidden Post-Translational Modification Sites
#bioinformatics #compchem #folding #proteindynamics
Protein Dynamics at Different Timescales Unlock Access to Hidden Post-Translational Modification Sites
Post-translational modifications (PTMs) alter the proteome in response to intra- and extracellular signals, providing fundamental information processing in development, homeostasis and disease. Here, ...
biorxiv.org
June 28, 2025 at 11:36 AM
Now published in Advanced Science: our latest study combining NMR and MD to investigate a transient folding intermediate of human lysozyme #nmrchat #compchem
June 25, 2025 at 12:04 PM
Reposted by Julian Streit
In press!! NMR & MD simulations reveal how non-native contacts stabilise a key transient intermediate in the lysozyme amyloid cascade. Well done Minkoo and all!! @phar.cam.ac.uk For CMD ❤️ advanced.onlinelibrary.wiley.com/doi/10.1002/...
Amyloid Forming Human Lysozyme Intermediates are Stabilized by Non‐Native Amide‐π Interactions
Mutational variants of human lysozyme cause fatal systemic amyloidosis by depositing kilograms of protein in the viscera of patients. Central to this process is a partially unfolded protein intermedi....
advanced.onlinelibrary.wiley.com
June 25, 2025 at 11:32 AM
Reposted by Julian Streit
The third episode of The Tortured Proteins Department is out now!

We chatted about grant cancellations, exciting regional meetings and reunions, two fun new preprints, community norms around code release, and the importance of giving kudos. @fraserlab.com
May 16, 2025 at 3:48 PM
Reposted by Julian Streit
Led by @vvouts.bsky.social in @rhp-lab.bsky.social, we measured the degron potency of >200,000 30-residue tiles from >5,000 cytosolic human proteins and trained an ML model for degrons

📜 www.biorxiv.org/content/10.1...
🖥️ github.com/KULL-Centre/...
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.
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...
www.biorxiv.org
May 15, 2025 at 12:44 PM
Reposted by Julian Streit
Rationally designing 19F probe pairs was key to determining the structures of protein folding intermediates on the ribosome in our latest preprint.

Our design strategy is now published in @natcomms.nature.com

www.nature.com/articles/s41...

#NMRchat #compbio #compchem
May 8, 2025 at 7:48 PM
Our latest is now in Nature Communications:
www.nature.com/articles/s41...
Rational design of fluorine NMR labelling sites (AlphaFold/molecular dynamics) to gain insights into protein structure and interactions for large complexes and in cells!
#NMRchat #compchem #AlphaFold #proteinfolding
LinkedIn
This link will take you to a page that’s not on LinkedIn
lnkd.in
May 8, 2025 at 8:01 PM
Reposted by Julian Streit
Presenting one of my favorite manuscripts I've ever worked on:

"Characterizing structural and kinetic ensembles of intrinsically disordered proteins using writhe"

www.biorxiv.org/content/10.1...

by Tommy Sisk, with a generative modeling component done in collaboration with @smnlssn.bsky.social
April 30, 2025 at 5:45 PM
Reposted by Julian Streit
AlphaFold is amazing but gives you static structures 🧊

In a fantastic teamwork, @mcagiada.bsky.social and @emilthomasen.bsky.social developed AF2χ to generate conformational ensembles representing side-chain dynamics using AF2 💃

Code: github.com/KULL-Centre/...
Colab: github.com/matteo-cagia...
April 17, 2025 at 7:11 PM
Excited to share our new preprint presenting mechanistic details of how proteins fold on the ribosome. With co-first author @sammyhschan.bsky.social , @twlodarski.bsky.social , Alkistis Mitropoulou, Lisa Cabrita, and John Christodoulou.
www.biorxiv.org/content/10.1...
#proteinfolding #compchem #NMR
April 11, 2025 at 7:50 PM
Reposted by Julian Streit
Structures of protein folding intermediates on the ribosome https://www.biorxiv.org/content/10.1101/2025.04.07.647236v1
April 11, 2025 at 6:48 PM
Reposted by Julian Streit
Cryo-EM, and integration with MD simulations, of nascent proteins on the ribosome.

Congrats Alki and @twlodarski.bsky.social and co-authors!
The ribosome directs nascent chains through two folding-dependent pathways https://www.biorxiv.org/content/10.1101/2025.04.08.647855v1
April 10, 2025 at 11:04 PM
Reposted by Julian Streit
Our paper on prediction of phase-separation propensities of disordered proteins from sequence is now published:
www.pnas.org/doi/10.1073/...

The paper has been substantially updated compared to the preprint including new experimental data and using the neural network to finetune CALVADOS. 1/n
March 25, 2025 at 5:54 PM
Reposted by Julian Streit
Gemma Solomon and I are looking for a postdoc to work across the two groups on modelling biological systems with a view to applications for quantum computing

More details about the project including how to apply in the link below. Deadline April 9 2025

candidate.hr-manager.net/ApplicationI...
March 22, 2025 at 7:16 PM
Reposted by Julian Streit
CALVADOS now has parameters for phosphorylated amino acids

@asrauh.bsky.social @giuliotesei.bsky.social and Gustav Hedemark used a top-down approach in which we targeted experimental data to derive parameters or phosphorylated serine and threonine doi.org/10.1101/2025...
March 21, 2025 at 6:59 AM
Reposted by Julian Streit
Structural biology is in an era of dynamics & assemblies but turning raw experimental data into atomic models at scale remains challenging. @minhuanli.bsky.social and I present ROCKET🚀: an AlphaFold augmentation that integrates crystallographic and cryoEM/ET data with room for more! 1/14.
February 24, 2025 at 12:23 PM
Reposted by Julian Streit
Preprint! The ribosome’s electro charge defines how proteins fold by all-atom MD and 19F NMR. Led by @julianstreit.bsky.social with @charles-burridge.bsky.social, Joel Wallace, @chriswaudby.bsky.social, Lisa Cabrita, John Christodoulou

#nmrchat #compchem #compbio

doi.org/10.1101/2025.02.10.637539
Long-range electrostatic forces govern how proteins fold on the ribosome
Protein biosynthesis and folding are tightly intertwined processes regulated by the ribosome and auxiliary factors. Nascent proteins can begin to fold on their parent ribosome but formation of the nat...
doi.org
February 15, 2025 at 1:44 PM