Sammy Chan
@sammyhschan.bsky.social
Postdoc at UCL studying protein folding on the ribosome, usually by 19F NMR scholar.google.com/citations?user=vE92YsgAAAAJ&hl=en&oi=sra
New online: Structures of protein folding intermediates on the ribosome
Structures of protein folding intermediates on the ribosome
Nature Structural & Molecular Biology, Published online: 16 June 2026; doi:10.1038/s41594-026-01814-7Atomistic structural ensembles of protein folding intermediates on the ribosome are resolved by comprehensive 19F nuclear magnetic resonance analyses integrated with molecular dynamics simulations, providing insights into cotranslational folding pathways.
dlvr.it
Excited to share our work describing structural ensembles of protein folding intermediates on the ribosome is now published in @natsmb.nature.com ! www.nature.com/articles/s41... Very grateful to co-first author @sammyhschan.bsky.social, our supervisor John Christodoulou and all our co-authors.
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
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
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
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
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
Rational design of 19F NMR labelling sites to probe protein structure and interactions - Nature Communications
Rational design of protein labelling sites for 19F NMR experiments using AlphaFold predictions and molecular dynamics simulations enables simple, direct analyses of protein structure and interactions ...
nature.com
Sammy Chan@sammyhschan.bsky.social · 2y agoOut now! How to rationally design 19F labels to study structures of large biomol complexes, incl in cells. Using engineered ring currents, and designed with MD and AF. With co-first author Julian Streit, and Saifu Daya and John Christodoulou. #nmrchat #compchem www.biorxiv.org/content/10.1...
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
Cryo-EM, and integration with MD simulations, of nascent proteins on the ribosome. Congrats Alki and @twlodarski.bsky.social and co-authors!
bioRxiv Biophysics@biorxiv-biophys.bsky.social · last yr.The ribosome directs nascent chains through two folding-dependent pathways https://www.biorxiv.org/content/10.1101/2025.04.08.647855v1
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
Check out our latest preprint on the role of the ribosome in the folding of its nascent polypeptides - an integrative study combining NMR experiments and atomistic simulations! #NMRchat #compchem #CompBio #ribosome #proteinfolding www.biorxiv.org/content/10.1...
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...
biorxiv.org
The ribosome lowers the entropic penalty of protein folding
The ribosome lowers the entropic penalty of protein folding
Nature, Published online: 07 August 2024; doi:10.1038/s41586-024-07784-4 Structures of the growing peptide chain on and off the ribosome reveal that the ribosome destabilizes the unfolded nascent chain, promoting the formation of partially folded intermediate states.
nature.com
Rational design of 19F NMR labelling sites to probe protein structure and interactions https://www.biorxiv.org/content/10.1101/2024.12.11.627779v1
Out now! How to rationally design 19F labels to study structures of large biomol complexes, incl in cells. Using engineered ring currents, and designed with MD and AF. With co-first author Julian Streit, and Saifu Daya and John Christodoulou. #nmrchat #compchem www.biorxiv.org/content/10.1...
Rational design of 19F NMR labelling sites to probe protein structure and interactions
Proteins are investigated in increasingly more complex biological systems, where 19F NMR is proving highly advantageous due to its high gyromagnetic ratio and background-free spectra. Its application ...
biorxiv.org