Abstract
Optical spectroscopy has contributed enormously to our knowledge of the structure and dynamics of atoms and molecules and is now emerging as a cornerstone of the gas-phase methods available for investigating biomolecular ions. This chapter focuses on the UV and visible spectroscopy of peptide and protein ions stored in ion traps. First, we discuss experimental set-ups, de-excitation mechanisms following photo-excitation in electronically excited states and principles of action spectroscopy. Then, we report action spectra for different classes of gas-phase peptides and proteins. The optical activity of proteins in the near UV is directly related to the electronic structure and optical absorption of aromatic amino acids (Trp, Phe and Tyr). Some proteins also show absorption in the visible range due to the presence of a prosthetic group. Influence of protein charge state, formation of radical aromatic amino acids and solvation on proteins’ visible and UV spectra is discussed.
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Antoine, R., Dugourd, P. (2013). UV–Visible Absorption Spectroscopy of Protein Ions. In: Brøndsted Nielsen, S., Wyer, J. (eds) Photophysics of Ionic Biochromophores. Physical Chemistry in Action. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-40190-9_8
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DOI: https://doi.org/10.1007/978-3-642-40190-9_8
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