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: "Intricate coupling between the transactivation and basic-leucine zipper domains governs phosphorylation of transcription factor ATF4 by casein kinase 2"
Our new publication is available online: "Structure elucidation of the elusive Enzyme I monomer reveals the molecular mechanisms linking oligomerization and enzymatic activity"
Our new publication is available online: "Disorder Mediated Oligomerization of DISC1 Proteins Revealed by Coarse-Grained Molecular Dynamics Simulations""