Probing membrane-peptide and membrane-protein interactions by pulsed EPR spectroscopy

With the successful establishment of a protocol to measure inter spin distances in peptides embedded in lipid membranes by means of pulsed EPR, our future goals will be to detect key parameters related to adaptation of model peptides, such as WALP and β-peptides, in various lipid environments with specific emphasis on the hydrophobic mismatch. Distance measurements in aligned membranes will reveal the tilt angle of peptide helices. Moreover, experiments at EPR high fields and frequency will give unique insight into the helix periodicity in peptides with different secondary structures.