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Tomek Wlodarski

@twlodarski.bsky.social

POLONEZ BIS Research Fellow in the Institute of Biochemistry and Biophysics PAS || Previously @UCL @Cambridge || @EMBO Fellow || Computational biophysicist || Protein folding on the ribosome || hiking/running || https://tomekwlodarski.com/

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Tomek Wlodarski@twlodarski.bsky.social · last mo.

Out now in #NAR! 🧬 I mapped the evolution of the ribosomal exit tunnel through the "eyes" of the nascent chain using MD simulations. How do the tunnel geometry, lateral branching, and chemical landscape change across 64 distinct ribosomes from the 3 domains of life? academic.oup.com/nar/article/...

Evolution of the ribosomal exit tunnel through the eyes of the nascent chain

Abstract. The exit tunnel is a universally conserved feature of the ribosome that directs the nascent polypeptide into the cellular environment and is invo

academic.oup.com

Sammy Chan@sammyhschan.bsky.social · 2mo ago

Now in Nature SMB: how do proteins fold while still being made? We solved all-atom structures of two ribosome-tethered folding intermediates—invisible to cryo-EM, seen only by ¹⁹F NMR. Thank you @julianstreit.bsky.social, John Christodoulou & co-authors! nature.com/articles/s41594-026-01814-7

Structures of protein folding intermediates on the ribosome - Nature Structural & Molecular Biology

Atomistic structural ensembles of protein folding intermediates on the ribosome are resolved by comprehensive 19F nuclear magnetic resonance analyses integrated with molecular dynamics simulations, pr...

nature.com

Tomek Wlodarski@twlodarski.bsky.social · 7mo ago

Just in time for 2026! 🎆 Presenting a nascent-centric view on the shape of the ribosomal exit tunnel topology, based on MD-derived occupancy maps for 55 distinct ribosomes. 🧶🧬🖥️ 📄 Read the preprint: biorxiv.org/content/10.6... #StructuralBiology #Ribosome #CryoEM #Evolution #Biophysics

Evolution of the ribosomal exit tunnel through the eyes of the nascent chain

The ribosomal exit tunnel is a universally conserved feature of the large subunit that directs the nascent polypeptide chain into the cellular environment and is involved in co-translational folding, ...

biorxiv.org

Janet Kumita@jrkumita.bsky.social · last yr.

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

Sammy Chan@sammyhschan.bsky.social · last yr.

Preprint! All-atom structures of 2 folding intermediates on the ribosome, along parallel pathways & conserved across Ig domains, by 19F NMR & MD Co-led by @julianstreit.bsky.social, & thanks twlodarski.bsky.social, Alki, Lisa & John Christodoulou! #nmrchat #compbio www.biorxiv.org/content/10.1...

Structures of protein folding intermediates on the ribosome

The ribosome biases the conformations sampled by nascent polypeptide chains along folding pathways towards biologically active states. A hallmark of the co-translational folding (coTF) of many protein...

biorxiv.org