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Florent Delhommel

@florentdelh.bsky.social

CNRS researcher in bio-NMR at the CBS, Montpellier. Mainly work on HSP90, but interested in everything structural biology and protein interactions. 😊

8 Posts514 Follower254 Folgt
Francois Jobard@francoisjobard.bsky.social · 4w ago

Dans le secteur de #Montpellier, c'est "barricadement quasi non stop de 11 h à 20 h depuis bientôt 1 mois (...). La Txm des 26 derniers jours s'élève à 36.6°C...On en arrive à espérer du 33/34°C pour souffler, je ne sais pas si vous vous rendez compte... " forums.infoclimat.fr/f/topic/6005...

Gaétan Heymes@gaetanheymes.bsky.social · 4w ago

A #Montpellier, la #chaleur est inédite, insupportable. Du 29 juin au 8 juillet 2026, la température moyenne est de 29,8°C à l'aéroport, soit une anomalie de +6,3°C. Jamais une telle température moyenne, ni une telle anomalie, n'avaient été observées depuis l'ouverture en 1946. 1/3

Matteo Paloni@betterwithchem.bsky.social · last mo.

Excited to share our new bioRxiv preprint with @matbocca.bsky.social and @davideerba.bsky.social! We use a minimal coarse grained model to investigate how protein-RNA binding affects RNP condensate formation. We'd love to hear your thoughts and feedback!

bioRxiv Biophysics@biorxiv-biophys.bsky.social · last mo.

Interplay Between Protein-RNA Binding and Phase Separation Drives Emergent Behavior in RNP Condensates https://www.biorxiv.org/content/10.64898/2026.06.25.734509v1

Leah Stokes@leahstokes.bsky.social · last mo.

The heatwave in Europe is so extreme, it's 25–32°F (14–18°C) above normal. You read that right. France recorded it's hottest day ever. The UK had its hottest ever June day. The ground is exceeding 122°F (50°C). People are dying. Tell me again why we shouldn't talk about climate change???

Philip Ball@philipcball.bsky.social · 2mo ago

I suspect it's not widely known that (or how much) genetic variation that would otherwise be deleterious is "hidden" by buffering. Much of that is accomplished by a protein called Hsp90. I've written a feature for Nature about it. www.nature.com/articles/d41...

These ‘master’ proteins protect us from deadly mutations — and could inspire new drugs

Biology has clever ways to mask the effects of potentially harmful gene mutations. Scientists are investigating how this ‘buffering’ works — and how to exploit it.

nature.com

Center for Structural Biology (CBS Montpellier)@cbsmontpellier.bsky.social · 2mo ago

New paper from the @cbsmontpellier.bsky.social "CF2H: a cell-free two-hybrid platform for rapid protein binder screening " now out in Nature Communications www.nature.com/articles/s41...

CF2H: a cell-free two-hybrid platform for rapid protein binder screening - Nature Communications

Faster and cheaper experimental screening methods will democratize and accelerate the identification of high-affinity binders with biomedical applications. Here the authors present Cell-Free Two-Hybri...

nature.com

Julien Capin@ju-cap.bsky.social · last yr.

You designed binders for your favourite protein and wish there was a way to experimentally screen them within 24h w/ only a set of pipettes and a plate reader? Check out our Cell-Free 2-Hybrid approach (CF2H) Full post: tinyurl.com/48cz5nb6 Preprint: www.biorxiv.org/cgi/content/...

Alexis Verger 🧬🧫🧪@alexis-verger.cpesr.fr · 4mo ago

With all the cuts to research funding in European countries, everyone is turning to the ERC... The ERC should be a source of supplementary funding, not a substitute. Every country in Europe must invest in basic research and increase its budgets!!!!

Dr Ino Agrafioti@inoagrafioti.bsky.social · 4mo ago

I don’t know if you saw the MASSIVE news announced by @erc.europa.eu today: from now on, if you get a B at step 1 you are eligible to apply at N+3(!!!) years. Say you got a B in STG2026 step 1, you thought you could apply in STG2028, but no: only in STG2029! erc.europa.eu/news-events/...

Angeliki Giannouli@angelikig.bsky.social · 4mo ago

✨ New paper out in #JACS! We looked at the intrinsically disordered CTD tail of #Hsp90 often seen as a passive linker. Turns out, it’s not. #StructuralBiology #Biophysics #EPR #NMR pubs.acs.org/doi/10.1021/...

Beyond a Passive Tether: Structural Insights into the Disordered Tail of Hsp90

The molecular chaperone Hsp90 is an abundant and essential homodimer that supports the stability and folding of hundreds of client proteins in cells. Its C-terminal domain (CTD) mediates dimerization and serves as a docking site for cochaperones bearing tetratricopeptide repeat (TPR) domains, which recognize the conserved MEEVD motif located at the end of an intrinsically disordered CTD tail. Despite its conservation, the structural role of this tail remains poorly understood. We investigated the conformational behavior of the yeast Hsp90 (yHsp90) CTD tail and its response to the binding of the TPR-containing PPIase cochaperone Cpr6. Using site-directed spin labeling with nitroxide and Gd(III) labels, we examined full-length yHsp90 (FL), isolated CTD (IsoC), and tail-truncated variants by double electron–electron resonance (DEER) and EPR spectroscopy. The CTD tails in IsoC and FL adopted distinct conformational ensembles, attributed to intramolecular interactions with the middle domain in FL. Cpr6 binding abolished these differences, indicating disruption of intramolecular tail contacts. In IsoC, the tail also stabilized an additional CTD conformation near the dimer interface that was absent in FL and was lost upon tail truncation, consistent with tail–CTD interactions observed by NMR. This population was reduced upon Cpr6 binding, shifting the IsoC conformational distribution toward that of FL. Additionally, this population was reduced in cellular environments and mimics. Together, our results demonstrate that the disordered CTD tail is an active structural element that modulates both its own conformational ensemble and CTD architecture, highlighting its potential functional relevance in the Hsp90 chaperone cycle.

pubs.acs.org

@paulschanda.bsky.social · 5mo ago

Returning from an amazing Proteostasis meeting, with lots of new ideas & grateful for great feedback about our mitochondrial-import work. Traveling back from Frankfurt to Vienna by train, I am reminded of the CO2-emissions savings of train vs. plane travel. Also in 2026, I won't take a plane.

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MadScientist@mads100tist.bsky.social · 6mo ago

This graph basically shows that the MSCA are, as of now, useless unless the EU governance does something about it 🧪

A graph titled "MSCA Postdoctoral Fellowships: section EF-LIF". The graph shows the scores between 70 and 100 over the years 2022, 2023, 2024 and 2025. The years 22, 23 and 24 show a relatively flat normal distribution that peaks at around 90ish and drops at both ends, more dramatically at 95+. The year 25, however, is very different: significant drop at the ends with a dramatic increase at ~95 (going from around 25 to 60ish %)
Natalie Schaworonkow@nschawor.bsky.social · 6mo ago

the cutoff scores for #MSCA postdoc fellowships are very high this year. has the score distribution shifted compared to previous years? I made a plot with scores from past years. if scores are at ceiling level, the process becomes essentially a lottery, because minor issues can lead to deductions.

Barack Obama@barackobama.bsky.social · 6mo ago

The killing of Alex Pretti is a heartbreaking tragedy. It should also be a wake-up call to every American, regardless of party, that many of our core values as a nation are increasingly under assault.

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Center for Structural Biology (CBS Montpellier)@cbsmontpellier.bsky.social · 7mo ago

Join us in Montpellier in June 2026 for the second edition of the European South Atlantic Biophysical conference #ESAB2026

GdR ImaBio 🔬@gdrimabio.bsky.social · 7mo ago

#ESAB2026 is opening ! 👉 Registration is now available for the second edition of the European South Atlantic Biophysical conference. 👉 esab2026.cbs.cnrs.fr @cnrs.fr @umontpellier.bsky.social @cbsmontpellier.bsky.social @iupab.bsky.social @picoquant.bsky.social @cecamevents.bsky.social

Molecular Cell @cp-molcell.bsky.social · 7mo ago

Online Now: The essential co-chaperone Sgt1 regulates client dwell time in the Hsp90 chaperone cycle Online now:

The essential co-chaperone Sgt1 regulates client dwell time in the Hsp90 chaperone cycle

Engler et al. define the Sgt1-specific domain as essential for the Sgt1 chaperone function in yeast. Through structural and biochemical analyses, they uncover unique interactions of Sgt1 with Hsp90 and client proteins that enhance client maturation efficiency. Sgt1 stabilizes Hsp90-client complexes by preventing their dissociation mediated by the co-chaperone Aha1.

dlvr.it

Integrative Biophysics of Membranes @CBS Montpellier@membranesbiophy.bsky.social · 8mo ago

Watch Robert Quast @rbquast.bsky.social from our Team presenting our work on single molecule #FRET on #GPCR in the first FBI Connect webainar !

France-BioImaging@france-bioimaging.bsky.social · 8mo ago

The replay of the 1st edition of FBI Connect is now available!◀️ In this webinar, we welcomed Robert Quast from the CBS in Montpellier. He presented his latest project and an unique multicolor smFRET technique to study GPCR dynamics! 🔗Watch it here: youtu.be/pgU_3VhMutk

Max Bonomi@bonomimax.bsky.social · 9mo ago

Don’t miss this opportunity to work with a fantastic mentor, a great team, in a beautiful city of France!

Center for Structural Biology (CBS Montpellier)@cbsmontpellier.bsky.social · 9mo ago

Postdoctoral position in the team of Alessandro Barducci in the CBS, focusing on multiscale simulations of RNA-driven condensates, with applications in synthetic biology. More information : www.cbs.cnrs.fr/images/jobs/... The position is expected to start in early 2026, with some flexibility.

Technische Universität München@tum.de · 9mo ago

Misfolded proteins can cause #Alzheimers, #Parkinsons and #Cancer. Johannes Buchner, part of the CHAPEROME team, receives an #ERC Synergy Grant to study how chaperone #proteins keep cells healthy: go.tum.de/904052 👏 #ERCSyG #biotechnology @erc.europa.eu 📷A. Heddergott

Highly endowed ERC Synergy Grant for Prof. Johannes Buchner

Disease-causing proteins – ERC Synergy Grant for research at TUM on the role of chaperone “helper proteins.”

go.tum.de