High-pressure NMR
Scaffold proteins
and disordered peptides
Evolution of
viral proteins
We study the mechanisms of folding, activation, fibrillation and evolution of proteins involved in neurodegenerative and infectious diseases.
We use a combination of Nuclear Magnetic Resonance (NMR) spectroscopy, X-ray crystallography, molecular dynamics simulations and bioinformatics techniques to characterize the structural and functional properties of these proteins at an atomistic level.
The detailed characterization of these complex mechanisms provides a molecular basis for the development of new therapeutic approaches.
Our new publication is available online: "Lessons from pressure denaturation of proteins"
Our new publication is available online: "Pushing the Limits of Structure-Based Models: Prediction of Non-globular Protein Folding and Fibrils Formation with Go-Model Simulations"
A new publication is available online: "Prediction of nearest neighbor effects on backbone torsion angles and NMR scalar coupling constants in disordered proteins"