Sarah Rauscher

3) This is a collaborative project with the @meshorer1 lab, and the @RauscherLab lab. Talking about @RauscherLab, they have recently presented an elaborate MD-based model of the effects of PEG on the FP mCherry, a work we took part in (see doi.org/10.1101/2024.0…).

It is almost happening - #BPS2025 - and we are happy to attend and present our research. A thread. 1) I will give a talk Saturday morning @ Biological Fluorescence subgroup, presenting the work spearheaded by the PhD student Khalil Joron, about

We are excited to share our recent simulation study by PhD student Ethan Lee describing the conformational states of the active site loops of the main protease (MPro) of SARS-CoV-2, featured on the cover of Biochemistry --

In this work, we use all-atom MD simulations to investigate the molecular basis for the difference between human and rhesus TRIM5α in their ability to restrict HIV. See our manuscript by Liam Haas-Neill, Deniz Meneksedag-Erol & Ibraheem Andeejani --

Our simulations study describing the conformational states of the active site loops of the main protease (MPro) of SARS-CoV-2 is now published in Biochemistry -- pubs.acs.org/doi/10.1021/ac…

IDPSeminars returns this week! Sign up here! idpseminars.com

We have an open position for studying two-pore domain potassium channels using MD simulations and single-particle Cryo-EM. Please help us spread the word: leibniz-fmp.softgarden.io/job/50703298?l…

The Department of Physics at the University of Toronto is recruiting candidates in Theoretical Biological Physics for a tenure track Assistant, Associate or Full Professor. UofT has a vibrant biophysics community -- please join us! physics.utoronto.ca/physics-at-uof…

If you want to see what a comprehensive computational analysis of SH2 domain structure and dynamics in an oncoprotein looks like, with a little HDX thrown in on the side, then this here @RauscherLab paper is for you!

@BerlowLab @klyshko_to Thanks, Rebecca!

@RauscherLab @klyshko_to Congratulations Sarah and Eugene on this exciting milestone!

Please join us in congratulating the first PhD graduate from the Rauscher lab, Dr. Eugene Klyshko @klyshko_to! We took a moment this week to celebrate his successful PhD defense.

Sharing our preprint - an investigation into the effects of an oncogenic driver mutation on the structure and dynamics of an SH2 domain. We tested our simulation predictions using HDX-MS experiments in collaboration with Derek Wilson at York University. @dkwilson2

Excited to share our recent simulation study on the main protease of SARS-CoV-2 — preprint on bioRxiv —

@eitan_lerner @Elishahaas1 @shiweiss @PSB_lab @dokhlab @meshorer1 Congratulations and well-deserved!

Just got the word: Tenured&promoted. Many thanks to my group members, with which we explored new concepts and ideas. Also, many thanks to my mentors/collaborators, esp. @Elishahaas1,@shiweiss,@PSB_lab,@dokhlab,@RauscherLab,@NirKeren316,@meshorer1 & Nir Kalisman.

Looking forward to this meeting!

@KatieWilsonA Congratulations! Well-deserved recognition. 🎉

So excited to be one of the 2024 Banting Discovery Awardees!! 🎉

📜 Just published online... 🎉- Single-particle #CryoEM and MD #simulations: A perfect match - by Lars @Pogoscience, Maxim @maxotubule and Helmut. sciencedirect.com/science/articl… Happy reading!

Say it louder for the people in the back. PEG is not inert! Looking forward to reading this one more in depth.

@CompBioPhys @eitan_lerner Thank you!

@RauscherLab @eitan_lerner Great news! Contrats to the team! 🎉

A recent manuscript, “PEG-mCherry interactions beyond classical macromolecular crowding,” by Liam Haas-Neill from our lab and Khalil Joron from the lab of @eitan_lerner is out, preprint on bioRxiv: biorxiv.org/content/10.110…

At high concentrations of PEG, we find that mCherry molecules associate to form large aggregates. By carrying out experiments with a bulkier crowder, dextran, we show that the effects of crowder-protein interactions depend on the crowder's chemical features and its bulkiness.

We find that PEG-wrapping around the side chains of lysine residues is prevalent, occurring in at least 20% of all crystal structures containing PEG, which corresponds to approximately 0.4% of all structures in the PDB.