In cooperation with the groups of Gert von Helden and Carsten Baldauf from the Fritz Haber Institute (FHI) of the Max Planck Society, we investigate peptides and proteins in the gas phase using infrared multiple photon dissociation (IRMPD) spectroscopy.
In the condensed phase IR spectroscopy is a well-established tool to analyze the structure and dynamics of proteins and their assemblies. This is based on the fact that the position of the characteristic amide I and amide II vibrational bands provides a direct measure of the molecules secondary structure. In the absence of solvent, IR spectra can also be measured using action spectroscopy techniques. The absence of reference values for species with defined conformation as well as the typical peak broadening observed for larger molecules, however, so far restricted the applicability of the method to small peptides with usually no more than ten residues. Here, we are aiming to extend the effective size-range of the method to folded proteins and protein complexes using conditions that are specifically optimized for retention of the molecules conformation in the gas phase. Tunable infra-red radiation for these experiments is provided by the FHI free electron laser.
Gas-phase IR spectra of intact α-helical coiled coil protein complexes
Pagel, K.; Kupser, P.; Bierau, F.; Polfer, N.C.; Steill, J.D.; Oomens, J.; Meijer, G.; Koksch, B.; von Helden, G.; Int. J. Mass Spectrom. 2009, 283, 161-168.