Schematic showing the function of Sgt1 in yeast.
Our latest work is now out in @cp-molcell.bsky.social !
We have looked at Sgt1, an essential Hsp90 co-chaperone in yeast. We determined its interaction with Hs90 and showed that it stabilises the chaperone-client complex and prevents its dissociation by Aha1.
www.cell.com/molecular-ce...
Wishing everyone happy holidays with a little glimpse at our festive Christmas party 🎄🎁
Congrats to our lab member Philipp, who defended his PhD this week! 🎓🎉
graphical abstract showing the combination of techniques used to analyze the dynamics of a de novo enzyme.
Our latest work is out! We combined #NMR with #Crystallography, #MD, and #ProteinMPNN to analyze the conformational dynamics of a de novo enzyme and redesigned it! Great collaboration between
@cathleenzeymer.bsky.social and the @sattler-lab.bsky.social.
www.cell.com/structure/fu...
Looking back on an inspiring and stimulating two days at the Ultra-Highfield NMR and 4D Structural Biology Symposium. Huge thanks to all speakers, participants, and organizers for making this such an insightful and engaging event! 🧲🧬
Biomolecular Breathing and the 4D View of Life: Insights from the BNMRZ Symposium
Biomolecular Breathing and the 4D View of Life
How do biomolecules breathe? This question was at the heart of the international #BNMRZ symposium, hosted by the Bavarian NMR Center – a joint infrastructure of #HelmholtzMunich and the @tum.de.
👉 Read more: t1p.de/dpfr7
#StructuralBiology #NMR #AI
Our work presented at the Ultra-Highfield NMR and 4D Structural Biology workshop www.bnmrz.org/4dstructbiol organized by @sattler-lab.bsky.social! @bussigio.bsky.social will show our works on #RNA dynamics integrating #MD, #SAXS, and #NMR and validating a #CASP16 target using #cryoEM data
#BNMRZ Symposium 2025
Ultra-Highfield NMR and 4D Structural Biology – From Mechanisms to Therapies
💻 Online attendance is still possible: t1p.de/zdr8j
👉 Further information: t1p.de/rjuz4
@tum.de
#StructuralBiology #CryoEM #AI #TherapeuticInnovations
A member of our group, Luca Sperotto, successfully defended his PhD last week. Congratulations Dr. Luca! 🎓
on the left a picture of a crystal and on the right the xray diffraction of that crystal generated using a synchotron.
Morning sky-friends! We are delighted to share some ‘hot off the xray’ images from our talented scientists, Dr André Mourão & Ting Deng. They produced this beautiful diffraction of a compound bound to one of our protein targets whilst working with @esrf.fr
BNMRZ Symposium Ultra-Highfield NMR and 4D Structural Biology – From Mechanisms to Therapies, November 6–7, 2025, TUM Institute for Advanced Study, Garching @ias-tum.bsky.social registration opens soon www.bnmrz.org/4dstructbiol #BNMRZ #NMRchat #NMR 🧲
Helmholtz Munich Joins Germany’s Instruct-ERIC Centre for Structural Biology
#HelmholtzMunich’s BNMRZ has joined Germany’s Instruct-ERIC Centre 🔬
Instruct-ERIC provides open access to advanced structural biology technologies. #BNMRZ advances innovation in #NMR methods, drug discovery, and imaging - boosting the German Centre’s capabilities.
👉 Read more: t1p.de/pjtyv
New paper in collaboration with the Förstemann Lab & Boekhoven Lab is out! Combining #NMR & mutational analysis, we characterize the unique features of the #Ago2 IDR region which drives Ago2/RNA #condensate formation.
doi.org/10.1093/nar/...
@clarahipp.bsky.social
One of our group members @clarahipp.bsky.social had the great opportunity to attend the Nobel Laureate Meeting last week in sunny Lindau ☀️
#lino25
📢 Paper with @sattler-lab.bsky.social now published in @narjournal.bsky.social ! doi.org/10.1093/nar/... We combine #NMR, #SAXS, and #MD to construct conformational ensembles, showing that A-to-I hyper-editing leads to significant structural dynamics. MD simulations by @piompons.bsky.social
Schematic of Hsp90's conformational cycle and the effect of Sgt1 that stabilizes the client's complex and prevents Aha1 binding.
New preprint is out! We've looked at the interactions of Sgt1 with Hsp90 in yeast and found some surprising results! We've also shown that in the presence of clients, Sgt1 prevents aha1 binding on Hsp90 and thus increases the substrate's dwell time. #NMR #chaperone
www.biorxiv.org/content/10.1...
