In addition come check out posters by Lynn Gu (Tuesday B36), Joshua Morse (Tuesday LB13), Mark Petersen (Tuesday B37), Darren Kahan (Sunday B99), Amir Bitran (Tuesday B43) and Eva Gerber (Sunday B70)
In addition come check out posters by Lynn Gu (Tuesday B36), Joshua Morse (Tuesday LB13), Mark Petersen (Tuesday B37), Darren Kahan (Sunday B99), Amir Bitran (Tuesday B43) and Eva Gerber (Sunday B70)
Amir Bitran is co chairing the protein folding and stability platform tomorrow (4 pm rooms 201-203) and giving a platform talk as part of that session at 4:45 pm
The Marqusee lab is at BPS2026 in San Francisco! Susan gave an invited talk yesterday at the biopolymers in vivo subgroup! Today, Eva Gerber is co chairing the protein dynamics/allostery platform (4 pm rooms 204-206) and giving a flash talk as part of that session at 5:50 pm
And congrats to Amir Bitran @amirbitran.bsky.social for receiving a poster prize, and to lab alum Sara Volz @saravolz.bsky.social for receiving both a poster prize AND best talk prize at the GRS!
So proud of Eva Gerber who gave a fantastic talk on her new high throughput method for probing folding stability/kinetics! Way to go Eva!
Both Eva and Amir are also presenting posters!
The Marqusee lab is at the 2026 protein folding Gordon Research seminar + conference! Amir will be giving a 10 min talk at the GRS today, while Eva will give a 10 min talk at the GRC on Tuesday! Susan will serve as a panelist on today's career panel at the GRS!
Our postdoc Amir Bitran @amirbitran.bsky.social is giving a talk tomorrow at the University of Chile, hosted by Marqusee lab alum and current U. chile faculty Yito Wilson! Feel free to join the talk (which will be largely in Spanish) by scanning the QR code below
Congrats to our current postdoc Amir on his latest publication with the Shakhnovich and Rodnina labs! Check out this thread about their really interesting study, combining all-atom simulation with experiment to reveal a protein's co-translational folding pathway at an atomistic level of detail
So thrilled to share that Susan was selected as a 2025 Protein Society Fellow!
This may inform our understanding of how proteins evolve to satisfy unique environmental constraints, such as resisting autolysis in the case of proteases. This has important implications in protein design as well
Protein energy landscapes affect not just how a protein first folds its structure, but also its functional and adaptive properties. In this work, Miriam performs a thorough biophysical characterization of how sequence changes affect the dynamics of two related proteases with different sequences
Excited to share our latest paper led by our talented former PhD student Miriam Hood
onlinelibrary.wiley.com/doi/10.1002/...
Update: Many congrats to our talented undergraduate student Joshua Morse for receiving a top poster award!!
In addition, come check out posters by Joshua Morse (T94), Darren Kahan (T82), Eva Gerber (F14), Mark Petersen (F77), Sophie Shoemaker (F89), Lynn Gu (F33), and Amir Bitran (S89)
Sophie Shoemaker will be giving a flash talk tomorrow afternoon in the "Proteins and Lipids: Fusion, Fission, Budding" session, while Eva Gerber will give a flash talk on Sunday as part of the morning "20 Amino Acidsโฆ and Beyond" session
Come check out presentations by the Marqusee lab at the 39th Protein Society Annual Symposium (@proteinsociety.bsky.social). Darren Kahan just gave an awesome talk on his work on IDPs.
Pleased to share a manuscript by our star former grad student, Sara Volz, showing the power of HDX-MS to probe folding intermediates of ฮณD crystallin under native conditions. This approach could shed future light on cataract-linked aggregation. Thanks @alexguseman.bsky.social and the Gronenborn lab
Check it out and let us know what you think! We are really excited by the combination of HDX-MS with eVLPs as it provides an opportunity to more easily study viral fusion proteins and other membrane proteins in native-like environments with HDX-MS.
7/7
D614G shifts the equilibrium to favor the prefusion conformation while the S2' site stays disordered. This study provides, to our knowledge, the first molecular explanation for the dual evolutionary advantages of furin cleavage and D614G.
6/7
However, furin cleavage also increases the population of the open-interface trimer, potentially promoting premature S1 shedding. We propose that this trade-off drove the evolution of the D614G mutation, an early fixed mutation in SARS-CoV-2.
5/7
We find that furin cleavage at the S1/S2 site increases the disorder of the S2โ protease site, which may increase TMPRSS2 activity leading to more efficient fusion. This provides a mechanistic explanation for furin cleavage enhancing infectivity.
4/7
We show that the native, full-length spike samples the previously identified open-interface trimer conformation, and its populations and interconversion rates are sensitive to sequence variations.
3/7
We use eVLPs to display full-length SARS-CoV-2 spike, both with and without prefusion-stabilizing prolines, and then probe dynamics with HDX-MS. Our findings reveal significant changes in spike dynamics resulting from natural and engineered variants.
2/7
Check out Sophie's new preprint on bioRxiv in collaboration with Magnus Hoffmann's lab where we conduct HDX-MS on SARS-CoV-2 spike proteins displayed on eVLPs to understand the dynamics of natural and engineered variants. 1/7 biorxiv.org/content/10.1...