We were excited to collaborate with Bruno Di Geronimo from @lynnkamerlin.bsky.social group on the stabilization of Salvia rosmarinus borneol dehydrogenase (BDH). In the preprint we explore two computational methods, put them into contrast and explore a subset of new variants. doi.org/10.64898/202...
Recent article from the lab published in @jacs.acspublications.org. Big congrats to first author Zainab Rashid for leading the study and great collaboration with @tomngrossmann.bsky.social and Jocelyne Vreede labs!😃
doi.org/10.1021/jacs...
#singlemolecule #dsRNA #RNAtherapeutics
Protein stabilization is a “Holy Grail” of biocatalysis, and stability design is an area of intense research interest. While it is increasingly feasible to effectively increase enzyme thermostability, optimization without compromising activity or selectivity remains a significant challenge. Here, we use full-atom protein sequence design with sidechain conditioning (FAMPNN) to engineer thermostable variants of the borneol dehydrogenase from Salvia rosmarinus (SrBDH1), an enzyme from a family where unselective enzymes dominate, and selectivity is determined by dynamical considerations. By combining FAMPNN design with residue conservation analysis and avoiding active site residues, we were able to computationally design SrBDH1 variants with up to 10 °C enhanced thermostability and strongly increased half-life time at elevated temperature, while retaining selectivity towards (+)-borneol. This design framework, integrating de novo and physics-based protein design tools, demonstrates that stability can be enhanced without disrupting functionally relevant dynamics, providing a route to engineer robust and selective biocatalysts.
Double-stranded RNA (dsRNA) has become an essential tool to understand biological processes with promising therapeutic implications. However, its usage is often limited due to poor cellular uptake and...
Now that our new @jacs.acspublications.org paper is printed, let me show you what's so cool about the group B [FeFe]-hydrogenase from Thermosediminibacter oceani (ToHydA) 😎
doi.org/10.1021/jacs...
David Dulin
Great to see our Highlight Review on TAV2b-derived RNA modulators online at Chemistry Letters doi.org/10.1093/chem...
Congrats to first author Marvin Albers! Read more about our RNA-targeting strategies also here:
-> doi.org/10.1002/anie...
-> doi.org/10.1093/nar/...
-> doi.org/10.1002/chem...
We report an #INCYPRO stabilised D-stereospecific hydrolase which operates efficiently at 50°C in 10% ethanol!
The article in Angewandte Chemie originates from a collaboration with the Bordusa Lab and Incircular. Congrats to all authors!
#ProteinEngineering #Biocatalysis
doi.org/10.1002/anie...
Excited to see our report on an #INCYPRO stabilised D-stereospecific hydrolase featured on the the inside cover of the current Angewandte issue! doi.org/10.1002/anie...
Congrats to all coauthors and collaborators from the Bordusa Lab and Incircular.
#ProteinEngineering #Biocatalysis
After a decade @vuamsterdam.bsky.social I’m excited to share that I’m starting @uni-goettingen.de
I’m incredibly grateful for my supportive colleagues at the VU and looking now forward to the opportunities ahead. Big THANKS to everyone in the group who supported our research over the years!
Stabilizing Proteins by Chemical Cross-Linking: Insights into Conformation, Unfolding, and Aggregation Using Native Ion Mobility Mass Spectrometry #AC pubs.acs.org/doi/10.1021/...
Greetings from the GRC on Artificial Molecular Switches and Motors! It’s exciting to see how the field has grown and is moving toward everyday applications—think photoswitchable tattoos!
The function and stability of proteins depend on their three-dimensional structure, which includes conformational dynamics and potential self-assembly. Protein structural organization is particularly ...
Next up, Jannik Keyser Paulus from the group of @tomngrossmann.bsky.social in @uni-goettingen.de focussed on redox responsive peptide dimers to stabilise and release therapeutic dsRNA
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#17GPS
