Sammy Chan
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sammyhschan.bsky.social
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
Reposted by Sammy Chan
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
Reposted by Sammy Chan
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
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
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...
www.biorxiv.org
April 11, 2025 at 7:45 PM
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
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
Reposted by Sammy Chan
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...
www.biorxiv.org
February 14, 2025 at 2:51 PM
Reposted by Sammy Chan
Rational design of 19F NMR labelling sites to probe protein structure and interactions https://www.biorxiv.org/content/10.1101/2024.12.11.627779v1
December 12, 2024 at 5:49 PM
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 ...
www.biorxiv.org
December 12, 2024 at 7:37 PM