We are developing novel methods to probe the interactions of TM helices in various lipid bilayer systems.
Lateral interactions between TM helices are in the very heart of the membrane protein folding problem. TM helices associate to give rise to membrane proteins with complex folds, such as ion channels and G-protein coupled receptors, performing intricate biochemical tasks.
We are developing novel methods to probe the interactions of TM helices in various lipid bilayer systems, such as lipid vesicles and surface-supported bilayers using Forster Resonance Energy Transfer (FRET).
The developed methodologies to measure free energies of homo- and heterodimerization are therefore important tools in the studies of membrane protein folding and the structure-function relationship for membrane proteins, as well as the molecular mechanisms behind human pathologies.