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Issue 34, 2011

Probing electrostatic interactions and structural changes in highly charged protein polyanions by conformer-selective photoelectron spectroscopy

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Abstract

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.

Graphical abstract: Probing electrostatic interactions and structural changes in highly charged protein polyanions by conformer-selective photoelectron spectroscopy

Supplementary files

Article information


Submitted
12 May 2011
Accepted
04 Jul 2011
First published
29 Jul 2011

Phys. Chem. Chem. Phys., 2011,13, 15554-15558
Article type
Paper

Probing electrostatic interactions and structural changes in highly charged protein polyanions by conformer-selective photoelectron spectroscopy

M. Vonderach, O. T. Ehrler, K. Matheis, T. Karpuschkin, E. Papalazarou, C. Brunet, R. Antoine, P. Weis, O. Hampe, M. M. Kappes and P. Dugourd, Phys. Chem. Chem. Phys., 2011, 13, 15554 DOI: 10.1039/C1CP21528K

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