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Journal Article

Charge-state resolved mid-infrared spectroscopy of a gas-phase protein

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Meijer,  Gerard
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Helden,  Gert von
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Citation

Oomens, J., Polfer, N., Moore, D. T., Meer, L. v. d., Marshall, A. G., Eyler, J. R., et al. (2005). Charge-state resolved mid-infrared spectroscopy of a gas-phase protein. Physical Chemistry Chemical Physics, 7(7), 1345-1348. doi:10.1039/b502322j.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0011-094D-2
Abstract
Infrared spectra of a 104 amino-acid protein in the gas phase as a function of its charge state are presented. The spectra contain clearly resolvable bands in the amide I and II spectral regions, as well as a band at 1483 cm–1, which is not observed in solution phase spectroscopy and is especially prominent for the higher charge states. Compared to solution, the amide I band is blue-shifted and the amide II band red-shifted, as expected for species in an environment with reduced hydrogen bonding. The band positions are suggestive of a mostly -helical structure of the protein and their widths are comparable to those in solution, suggesting a similar conformational distribution.