#CheMelt
🔥 New from our group in Protein Science!

We introduce CheMelt, a tool for analyzing thermal & chemical protein denaturation, integrated into the EMBL Hamburg eSPC platform.

📖 Read the paper:
onlinelibrary.wiley.com/doi/10.1002/...

@embl.org @cssbhamburg.bsky.social
@au.dk

#Biophysics #CheMelt
Global analysis of thermal and chemical denaturation using <fc>CheMelt</fc>: Thermodynamic dissection of highly thermostable de novo designed proteins
De novo protein design often produces thermostable proteins that denature above 100°C, which complicates the analysis of their stability. Thermostable proteins can be unfolded by combined chemical an...
onlinelibrary.wiley.com
September 30, 2026 at 2:56 PM
First and foremost. @osvalb.bsky.social has done an amazing job of improving CheMelt - a new GUI for analysis of combined thermal and chemical denaturation data.
Thank you to reviewers for detailed feedback and to @osvalb.bsky.social for putting in the hard work!

bsky.app/profile/osva...
Do you want to study the stability of a designed protein that doesn't unfold below 90 ºC 🔥? Combine a denaturant and temperature and then analyse the results with our newest tool: CheMelt 🧪

Online:
- spc.embl-hamburg.de/app/chemelt
As Docker image (faster):
- hub.docker.com/r/emblspc/ch...
September 30, 2026 at 1:43 PM
Thermodynamic analysis of nanoDSF data is easy in principle, but difficult in practice.

@spcembl.bsky.social established a web-based GUI for global analysis of combined thermal and chaotrope denaturant by nanoDSF: CheMelt hosted by @embl.org in their eSPC package:

spc.embl-hamburg.de/app/chemelt
Chemelt - Default
spc.embl-hamburg.de
April 10, 2026 at 6:38 AM
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
April 10, 2026 at 9:38 AM
Global analysis of thermal and chemical denaturation using CheMelt: Thermodynamic dissection of highly thermostable de novo designed proteins https://www.biorxiv.org/content/10.64898/2026.04.07.716910v1
April 9, 2026 at 10:48 PM
Do you want to study the stability of a designed protein that doesn't unfold below 90 ºC 🔥? Combine a denaturant and temperature and then analyse the results with our newest tool: CheMelt 🧪

Online:
- spc.embl-hamburg.de/app/chemelt
As Docker image (faster):
- hub.docker.com/r/emblspc/ch...
June 10, 2026 at 3:11 PM
Global analysis of thermal and chemical denaturation using CheMelt: Thermodynamic dissection of highly thermostable de novo designed proteins https://www.biorxiv.org/content/10.64898/2026.04.07.716910v1
April 9, 2026 at 10:48 PM
Moreover, the errors of the fitted parameters can be easily estimated through leave-one-out or profile likelihood analysis (thank you reviewer #3) 😁
June 10, 2026 at 3:11 PM
And fitted (both 330 nm and 350 nm) with a global model to obtain estimates of ΔCp, ΔHm, Tm and the m-value.
June 10, 2026 at 3:11 PM
CheMelt expands the work done by Hamborg et al., (2020). Global analysis of protein stability by temperature and chemical denaturation. Analytical biochemistry.

For example, they kindly provide an unfolding dataset of the ACBP protein which can be imported in CheMelt:
June 10, 2026 at 3:11 PM