Associate Professor, Computational biophysicist @UofT @UTM_CPS https://xitter.cf/t.co/KIIYCdYIKj @sarahrauscher (🦋)

Toronto, Ontario
Joined August 2018
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/10.1101/2024.05.07.5…).
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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
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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 --
New issue! 📣 Read up on biased signaling, RNA editing, gut microbes, antibiotics and more! pubs.acs.org/toc/bichaw/64/1 Cover art: Lee & Rauscher @UofT explore flexible loops in the main protease of SARS-CoV-2, with implications for drug discovery. pubs.acs.org/doi/10.1021/acs…
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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 --
An all-atom view into the disordered interaction interface of the TRIM5α PRYSPRY domain and the HIV capsid biorxiv.org/cgi/content/shor… #biorxiv_biophys
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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/acs…
Excited to share our recent simulation study on the main protease of SARS-CoV-2 — preprint on bioRxiv —
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Sarah Rauscher retweeted
IDPSeminars returns this week! Sign up here! idpseminars.com
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Sarah Rauscher retweeted
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/jo…
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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-…
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Sarah Rauscher retweeted
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!
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
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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.
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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
The structural influence of the oncogenic driver mutation N642H in the STAT5B SH2 domain biorxiv.org/cgi/content/shor… #biorxiv_biophys
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Excited to share our recent simulation study on the main protease of SARS-CoV-2 — preprint on bioRxiv —
The Conformational Space of the SARS-CoV-2 Main Protease Active Site Loops is Determined by Ligand Binding and Interprotomer Allostery biorxiv.org/cgi/content/shor… #biorxiv_biophys
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Looking forward to this meeting!
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📜 Just published online... 🎉- Single-particle #CryoEM and MD #simulations: A perfect match - by Lars @Pogoscience, Maxim @maxotubule and Helmut. sciencedirect.com/science/ar… Happy reading!
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Sarah Rauscher retweeted
Say it louder for the people in the back. PEG is not inert! Looking forward to reading this one more in depth. – at Bethesda, MD
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/10.1101/…
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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/10.1101/…
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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.
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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.
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