Probing electrostatic interactions and structural changes in highly charged protein polyanions by conformer-selective photoelectron spectroscopy
Literature Information
Matthias Vonderach, Oli T. Ehrler, Katerina Matheis, Tatjana Karpuschkin, Evangelos Papalazarou, Claire Brunet, Rodolphe Antoine, Patrick Weis, Philippe Dugourd
We have recorded the first conformer-selective photoelectron spectra of a protein polyanion in the gas-phase. Bovine cytochrome c protein was studied in 8 different negative charge states ranging from 5− to 12−. Electron binding energies were extracted for all charge states and used as a direct probe of intramolecular Coulomb repulsion. Comparison of experimental results with simulations shows that the experimental outcome can be reproduced with a simple electrostatic model. Energetics are consistent with a structural transition from a folded to an unfolded conformational state of the protein as the number of charges increases. Furthermore, the additional ion-mobility data show that the onset of unfolding can be assigned to charge state 6− where three conformers can be distinguished.
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