Dr. van Mierlo leads the Protein Folding group. This group focuses on experimental elucidation of how proteins fold, on probing energy landscapes of protein folding, and on protein misfolding and its potentially harmful consequences. Use is made of advanced heteronuclear NMR spectroscopy and of hydrogen/deuterium exchange methodologies, as well as of fluorescence spectroscopic techniques, like Förster resonance energy transfer (FRET) and time-resolved anisotropy.
Protein-folding related projects tackled include:
- Bovine pancreatic trypsin inhibitor folding
- Adsorption-induced protein unfolding of alpha-lactalbumin
- Unfolding and aggregation in a complex mixture of proteins from potato
- Formation of beta-lactoglobulin fibers
- Unravelling the molecular basis of the stability of a hyperthermostable endo-beta-1,3-glucanase
- Folding behaviour of a transmembrane segment of the proton translocation channel of V-ATPase
- Flavoprotein folding, with flavodoxin as particular example.
Recently, a research line concerning the elucidation of folding events of a flavoprotein on the ribosomal nanomachinery has started. Gaining knowledge about protein folding within, and just outside, the ribosomal exit tunnel is strongly required to enhance our understanding of protein folding in the cell, and to obtain insights into factors responsible for protein misfolding, aggregation, and, potentially, for numerous devastating pathologies.