Conformer-selective photoelectron spectroscopy of alpha-lactalbumin derived multianions in the gas phase

Abstract : We have recorded conformer-selective, gas-phase photoelectron spectra of a-lactalbumin derived multianions generated by electrospraying solutions of both the native protein and its denatured form (as prepared by breaking the sulfur-sulfur bonds by chemical reduction). Three different groups of gas-phase multianion conformers have been observed and characterized. Highly-folded and partially-unfolded structures are obtained from solutions of the native protein. Only highly-elongated conformers are observed upon electrospraying the denatured protein. Adiabatic detachment energies were determined at several negative charge states for each conformer group. In comparison to highly-elongated conformations, highly-folded structures show a steeper decrease of electron binding energy with increasing negative charge. By comparing experimental detachment energies for highly-elongated structures with the predictions of a simple electrostatic model calculation, we have determined the effective dielectric shielding constant.
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Submitted on : Monday, March 3, 2014 - 12:00:00 PM
Last modification on : Thursday, September 6, 2018 - 3:12:04 PM

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Matthias Vonderach, Marc-Oliver Winghart, Luke Macaleese, Fabien Chirot, Rodolphe Antoine, et al.. Conformer-selective photoelectron spectroscopy of alpha-lactalbumin derived multianions in the gas phase. Physical Chemistry Chemical Physics, Royal Society of Chemistry, 2014, 16 (7), pp.3007-3013. ⟨10.1039/c3cp54596b⟩. ⟨hal-00954595⟩

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