New preprint out 🚀
De novo designed proteins are often too stable — but why?
Using CheMelt, we show that their exceptional thermostability is largely driven by unusually low heat capacity changes (ΔCp).
👉 www.biorxiv.org/content/10.6...
@embl.org @osvalb.bsky.social @proteinmagnus.bsky.social
Why are de novo designed proteins so extremely thermostable?
We try to answer this question by dissecting the thermodynamics of unfolding of mini-binders emerging from our protein design pipeline – and establish a convenient GUI for data analysis in the process.
doi.org/10.64898/202...
New protocol out now! 📕🖊️🔍
A practical workflow for analyzing CD thermal unfolding of short RNAs — from SVD decomposition to two-state fitting to extract melting temp and enthalpy with ChiraKit.
A must-see if you’re working with RNA structure and CD data.
DOI: 10.1007/978-1-0716-5084-4_12 
New on bioRxiv 🧪 📄
A fresh look at how domain-specific ligand binding controls TRPM2 activation ⛓️💥
This work disentangles the roles of distinct nucleotide-binding domains and their contribution to gating — a long-standing question in the field. 
👉 www.biorxiv.org/content/10.6...
@embl.org
Excited to be attending the Biennial Conference of Instruct-ERIC in Brussels.
@instruct-eric.bsky.social
Looking forward to engaging discussions on structural biology, research infrastructures, technology development, and scientific collaboration across Europe.
@embl.org
@cssbhamburg.bsky.social
Very exciting demo on smFRET &FCCS measurements in our SPC facility this week with Exciting Instruments @ei-science.bsky.social ✨🧮
Thank you for allowing us to measure single molecule resolution using your technology.
It has been again, very exciting 🔍🤩
@embl.org @cssbhamburg.bsky.social
The analysis tool is part of the eSPC package developed by @osvalb.bsky.social & @spcembl.bsky.social from EMBL Hamburg.
User-friendly analysis software for many biophysical techniques. Typically the eSPC software is better than that provided with the instrument:
spc.embl-hamburg.de
