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Levy_research_group @koby_group

Exploring molecular dynamics to uncover the mechanisms of DNA, RNA, proteins and their interactions. #MDsimulations #StructuralBiology Dept, #WeizmannInstitute

Joined September 2023
  • Tweets 14
  • Following 168
  • Followers 29
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Levy_research_group retweeted
Liam M. Longo@LiamLongo
28 Mar 2025
Functional Ambidexterity of an Ancient Nucleic Acid-Binding Domain Now out now in @angew_chem Exciting collaboration with @Metanis_Group and @koby_group onlinelibrary.wiley.com/doi/…

Functional Ambidexterity of an Ancient Nucleic Acid‐Binding Domain

The (HhH)2-Fold is an ancient and ubiquitous nucleic acid-binding domain. We demonstrate that this domain, which interacts with the minor groove of dsDNA, is functionally ambidextrous – that it can...

onlinelibrary.wiley.com
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Our study with @rogoulenko in @NAR_Open shows #DNA flexibility impacts protein binding. Despite kinetic challenges, evolution ensures proteins effectively target and bind DNA. Check out Daniel Philosoph's cover art, hand-painted with real brushes! #ProteinDNA #ProteinStructures
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🎉 Excited to share our latest publication jctc "Histidine in Proteins: pH-Dependent Interplay between π–π, Cation–π, and CH–π Interactions" by @rivkacalinsky. Discover more: (pubs.acs.org/doi/10.1021/acs…) #ComputationalChemistry #Histidine #MolecularSwitch #CationPi

Histidine in Proteins: pH-Dependent Interplay between π–π, Cation–π, and CH–π Interactions

Histidine (His) stands out as the most versatile natural amino acid due to its side chain’s facile propensity to protonate at physiological pH, leading to a transition from aromatic to cationic...

pubs.acs.org
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Levy_research_group retweeted
Shifra Lansky@ShifraLansky
17 Jun 2024
I have just opened my lab at the Weizmann Institute of Science, Department of Chemical and Structural Biology, and am looking for students! Please share! :) For more details, check out my website: weizmann.ac.il/CSB/lansky
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Our paper on the strong interplay between DNA deformability and protein binding has just appeared. It is not just about the extensive search or the energetic barrier for binding but the delays due to many unproductive binding events. academic.oup.com/nar/advance…

Skipping events impose repeated binding attempts: profound kinetic implications of protein–DNA...

Abstract. The kinetics of protein–DNA recognition, along with its thermodynamic properties, including affinity and specificity, play a central role in shap

academic.oup.com
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"Exciting news! @segevnaveh from our group, contributed molecular dynamics simulations to understand more about the ORC DNA binding. Check out the highlights of our latest paper led by Michal Chappleboim from the @BarkaiLab in @NAR_Open. #research #science"
Barkai Lab@BarkaiLab
13 Apr 2024
Exciting news! Our latest paper "Ordered and disordered regions of the Origin Recognition Complex direct differential in vivo binding at distinct motif sequences", led by Michal Chappleboim is now out in @NAR_Open. Check out the highlights below. doi.org/10.1093/nar/gkae249
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Levy_research_group retweeted
Department of Chemistry, IIT Jodhpur@Chemistry_IITJ
15 Mar 2024
Hello All, Delighted to share with you the 3rd lecture of our Webinar Series (On March 20th at 5 PM IST; open to all) by Prof. Koby Levy! For details please visit: sites.google.com/iitj.ac.in/…"
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Levy_research_group retweeted
Weizmann Institute
@WeizmannScience
1 Feb 2024
Congratulations to Prof. Koby Levy, the new Head of Chemical and Structural Biology Department @koby_group
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Levy_research_group retweeted
Jan Jensen (janhjensen.bsky.social)@janhjensen
5 Oct 2023
New preprint: Automated Quantum Chemistry for Estimating Nucleophilicity and Electrophilicity with Applications to Retrosynthesis and Covalent Inhibitors doi.org/10.26434/chemrxiv-20… #compchem with @ReeNicolai and Andreas Göller Try it out here: esnuel.org
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Here is our recently published paper about proline, “Not Only Expansion”. Thank you @milan_hazra_90 for this work. It got cover magazine at jmb magazine! #moleculardynamics #proline #idr doi.org/10.1016/j.jmb.2023.1…
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in predicting IDR dimension as a function of their abundance and density in sequences. Outlooks fetched from extensive atomistic simulations of small peptides were fed to calibrate a CG model which could reproduce the effect of prolines in real IDRs.
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