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: "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"
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