Giorgos Gouridis

Our research focuses in understanding the intimate structure-function interconnection in biomolecules. For this, we decrypt at the molecular level their structural dynamics.
Protein structural dynamics occur constantly in living cells enabling every protein to perform its tasks and are finely regulated and orchestrated by binding interactions with their partners and/or their respective substrates. Altered protein dynamics lead to cellular malfunction, disease and death. Thus, monitoring those allows us to derive the molecular etiology of human diseases.
Structural dynamics, apart from revealing how proteins function, they also dictate the means by which proteins evolve to compute distinct functions.

The aim of our group, to understand life and evolution at the molecular level, is persuaded by studying protein folding, binding and dynamics. The folding funnel model that is rooted in the free energy landscape theory is the most widely accepted one to describe all 3 life processes, as the only difference between them is chain connectivity. Our labs’ holly-grail is to: (i) Find the key structural elements and understand how such modulate the depth of the energy valleys, (ii) Understand how such elements modulate the enthalpic-entropic factors to by-pass the transition barriers and ultimately (iii) How these elements vary during evolution to confer distinct functions and substrate specificities.

For this, we are coupling “traditional” biochemical/molecular biology tools to an array of powerful (bio)physical procedures (e.g. smFRET, HDX-MS, ITC) and combine the experimental outcome with molecular dynamic simulations (e.g. Gromacs).