Switch Laboratory is an independent research group supported by the Flanders Interuniversity Institute for Biotechnology (VIB), located at the Free University of Brussels (VUB).

Our research is geared on 3 topics that closely interact:

1. protein (mis)folding, aggregation and amyloidosis with a particular attention for aggregation gatekeepers
2. protein dynamics and signal transduction: how do conformational fluctuations of the native state achieve signal transduction and allostery?
3. the effect of SNPs on the molecular phenotype of proteins: how does human genetic variability affect protein conformation and function?

The questions we want to address require a multidisciplinary approach that combines in vitro biophysical techniques and computational structural biology methods with cell biological studies. We have developed our own computational algorithms to predict protein stability and folding (FOLDX), aggregation and amyloidosis (TANGO) and chaperone interaction (LIMBO) and used these tools to build a database that describes the molecular phenotype of all non-synonymous coding human SNPs (SNPeffect). To study the biophysical properties of proteins we use different biophysical methods including fluorescence, circular dichroism, Fourier-transform infrared spectroscopy, static and dynamic light scattering, differential scanning and isothermal calorimetry, stopped-flow kinetics and electron microscopy. To study the interaction of protein aggregates with cells we use standard cellular assays and perform fluorescence microscopy on mammalian cell cultures.