Sarah Rauscher

Associate Professor, Computational biophysicist @UofT @UTM_CPS
@sarahrauscher (🦋)

[EitanLernerLab @eitan_lerner]

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 https://t.co/pUFSi5xryT).

[EitanLernerLab @eitan_lerner]

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

[Sarah Rauscher @RauscherLab]

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 --

[Biochemistry @BiochemistryACS]

New issue! 📣

Read up on biased signaling, RNA editing, gut microbes, antibiotics and more!

https://t.co/i9Qi7EhtJQ

Cover art: Lee & Rauscher @UofT explore flexible loops in the main protease of SARS-CoV-2, with implications for drug discovery.

https://t.co/DLJy7Fw0Wb

[Sarah Rauscher @RauscherLab]

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 --

[bioRxiv Biophysics @biorxiv_biophys]

An all-atom view into the disordered interaction interface of the TRIM5α PRYSPRY domain and the HIV capsid https://t.co/GsCZsUcs15 #biorxiv_biophys

[Sarah Rauscher @RauscherLab]

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 --
https://t.co/03cGhbhzOx

[Sarah Rauscher @RauscherLab]

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

[IDPseminars @IDPseminars]

IDPSeminars returns this week! Sign up here! https://t.co/gqqT06y8mE

[HanSun_lab @HanSun_lab]

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: https://t.co/u0mN2zAmF3

[Sarah Rauscher @RauscherLab]

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!

https://t.co/yHhdKosaR9

[Derek Wilson @dkwilson2]

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!

[Sarah Rauscher @RauscherLab]

@BerlowLab @klyshko_to Thanks, Rebecca!

[Sarah Rauscher @RauscherLab]

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.

[Sarah Rauscher @RauscherLab]

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

[bioRxiv Biophysics @biorxiv_biophys]

The structural influence of the oncogenic driver mutation N642H in the STAT5B SH2 domain https://t.co/YiBzYBfprU #biorxiv_biophys

[Sarah Rauscher @RauscherLab]

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

[bioRxiv Biophysics @biorxiv_biophys]

The Conformational Space of the SARS-CoV-2 Main Protease Active Site Loops is Determined by Ligand Binding and Interprotomer Allostery https://t.co/7sd7XEbiZO #biorxiv_biophys

[Sarah Rauscher @RauscherLab]

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

[Sarah Rauscher @RauscherLab]

Looking forward to this meeting!

[Sarah Rauscher @RauscherLab]

@KatieWilsonA Congratulations! Well-deserved recognition. 🎉

[Theoretical & Computational Biophysics Department @CompBioPhys]

📜 Just published online... 🎉- Single-particle #CryoEM and MD #simulations: A perfect match - by Lars @Pogoscience, Maxim @maxotubule and Helmut. https://t.co/XyvtZTJe4V Happy reading!

[Alex Guseman @AlexGuseman]

Say it louder for the people in the back.

PEG is not inert!

Looking forward to reading this one more in depth.

[Sarah Rauscher @RauscherLab]

@CompBioPhys @eitan_lerner Thank you!

[Sarah Rauscher @RauscherLab]

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:
https://t.co/hclyzC01KZ

[Sarah Rauscher @RauscherLab]

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.

[Sarah Rauscher @RauscherLab]

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.