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Ultraviolet action spectroscopy of iodine labeled peptides and proteins in the gas phase

Journal Article


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Abstract


  • Structural investigations of large biomolecules in the gas phase are challenging. Herein, it is reported that action spectroscopy taking advantage of facile carbon–iodine bond dissociation can be used to examine the structures of large molecules, including whole proteins. Iodotyrosine serves as the active chromophore, which yields distinctive spectra depending on the solvation of the side chain by the remainder of the molecule. Isolation of the chromophore yields a double featured peak at 290 nm, which becomes a single peak with increasing solvation. Deprotonation of the side chain also leads to reduced apparent intensity and broadening of the action spectrum. The method can be successfully applied to both negatively and positively charged ions in various charge states, although electron detachment becomes a competitive channel for multiply charged anions. In all other cases, loss of iodine is by far the dominant channel which leads to high sensitivity and simple data analysis. The action spectra for iodotyrosine, the iodinated peptides KGYDAKA, DAYLDAG, and the small protein ubiquitin are reported in various charge states.

Authors


  •   Kirk, Benjamin B. (external author)
  •   Trevitt, Adam J.
  •   Blanksby, Stephen J. (external author)
  •   Tao, Yuanqi (external author)
  •   Moore, Benjamin N. (external author)
  •   Julian, Ryan (external author)

Publication Date


  • 2013

Citation


  • Kirk, B. B., Trevitt, A. J., Blanksby, S. J., Tao, Y., Moore, B. N. & Julian, R. (2013). Ultraviolet action spectroscopy of iodine labeled peptides and proteins in the gas phase. The Journal of Physical Chemistry Part A: Molecules, Spectroscopy, Kinetics, Environment and General Theory, 117 (6), 1228-1232.

Scopus Eid


  • 2-s2.0-84873889729

Ro Full-text Url


  • http://ro.uow.edu.au/cgi/viewcontent.cgi?article=1386&context=smhpapers

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers/374

Has Global Citation Frequency


Number Of Pages


  • 4

Start Page


  • 1228

End Page


  • 1232

Volume


  • 117

Issue


  • 6

Place Of Publication


  • United States

Abstract


  • Structural investigations of large biomolecules in the gas phase are challenging. Herein, it is reported that action spectroscopy taking advantage of facile carbon–iodine bond dissociation can be used to examine the structures of large molecules, including whole proteins. Iodotyrosine serves as the active chromophore, which yields distinctive spectra depending on the solvation of the side chain by the remainder of the molecule. Isolation of the chromophore yields a double featured peak at 290 nm, which becomes a single peak with increasing solvation. Deprotonation of the side chain also leads to reduced apparent intensity and broadening of the action spectrum. The method can be successfully applied to both negatively and positively charged ions in various charge states, although electron detachment becomes a competitive channel for multiply charged anions. In all other cases, loss of iodine is by far the dominant channel which leads to high sensitivity and simple data analysis. The action spectra for iodotyrosine, the iodinated peptides KGYDAKA, DAYLDAG, and the small protein ubiquitin are reported in various charge states.

Authors


  •   Kirk, Benjamin B. (external author)
  •   Trevitt, Adam J.
  •   Blanksby, Stephen J. (external author)
  •   Tao, Yuanqi (external author)
  •   Moore, Benjamin N. (external author)
  •   Julian, Ryan (external author)

Publication Date


  • 2013

Citation


  • Kirk, B. B., Trevitt, A. J., Blanksby, S. J., Tao, Y., Moore, B. N. & Julian, R. (2013). Ultraviolet action spectroscopy of iodine labeled peptides and proteins in the gas phase. The Journal of Physical Chemistry Part A: Molecules, Spectroscopy, Kinetics, Environment and General Theory, 117 (6), 1228-1232.

Scopus Eid


  • 2-s2.0-84873889729

Ro Full-text Url


  • http://ro.uow.edu.au/cgi/viewcontent.cgi?article=1386&context=smhpapers

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers/374

Has Global Citation Frequency


Number Of Pages


  • 4

Start Page


  • 1228

End Page


  • 1232

Volume


  • 117

Issue


  • 6

Place Of Publication


  • United States