Infrared Spectroscopy of Mobility-Selected H(+)-Gly-Pro-Gly-Gly (GPGG). Masson, A.; Kamrath, M., Z.; Perez, M., A., S.; Glover, M., S.; Rothlisberger, U.; Clemmer, D., E.; and Rizzo, T., R. Journal of the American Society for Mass Spectrometry, 6, 2015.
Infrared Spectroscopy of Mobility-Selected H(+)-Gly-Pro-Gly-Gly (GPGG). [pdf]Paper  Infrared Spectroscopy of Mobility-Selected H(+)-Gly-Pro-Gly-Gly (GPGG). [link]Website  abstract   bibtex   
We report the first results from a new instrument capable of acquiring infrared spectra of mobility-selected ions. This demonstration involves using ion mobility to first separate the protonated peptide Gly-Pro-Gly-Gly (GPGG) into two conformational families with collisional cross-sections of 93.8 and 96.8 Å(2). After separation, each family is independently analyzed by acquiring the infrared predissociation spectrum of the H2-tagged molecules. The ion mobility and spectroscopic data combined with density functional theory (DFT) based molecular dynamics simulations confirm the presence of one major conformer per family, which arises from cis/trans isomerization about the proline residue. We induce isomerization between the two conformers by using collisional activation in the drift tube and monitor the evolution of the ion distribution with ion mobility and infrared spectroscopy. While the cis-proline species is the preferred gas-phase structure, its relative population is smaller than that of the trans-proline species in the initial ion mobility drift distribution. This suggests that a portion of the trans-proline ion population is kinetically trapped as a higher energy conformer and may retain structural elements from solution. Graphical Abstract ᅟ.
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 title = {Infrared Spectroscopy of Mobility-Selected H(+)-Gly-Pro-Gly-Gly (GPGG).},
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 year = {2015},
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 websites = {http://www.ncbi.nlm.nih.gov/pubmed/26091889},
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 accessed = {2015-06-27},
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 abstract = {We report the first results from a new instrument capable of acquiring infrared spectra of mobility-selected ions. This demonstration involves using ion mobility to first separate the protonated peptide Gly-Pro-Gly-Gly (GPGG) into two conformational families with collisional cross-sections of 93.8 and 96.8 Å(2). After separation, each family is independently analyzed by acquiring the infrared predissociation spectrum of the H2-tagged molecules. The ion mobility and spectroscopic data combined with density functional theory (DFT) based molecular dynamics simulations confirm the presence of one major conformer per family, which arises from cis/trans isomerization about the proline residue. We induce isomerization between the two conformers by using collisional activation in the drift tube and monitor the evolution of the ion distribution with ion mobility and infrared spectroscopy. While the cis-proline species is the preferred gas-phase structure, its relative population is smaller than that of the trans-proline species in the initial ion mobility drift distribution. This suggests that a portion of the trans-proline ion population is kinetically trapped as a higher energy conformer and may retain structural elements from solution. Graphical Abstract ᅟ.},
 bibtype = {article},
 author = {Masson, Antoine and Kamrath, Michael Z and Perez, Marta A S and Glover, Matthew S and Rothlisberger, U and Clemmer, David E and Rizzo, Thomas R},
 journal = {Journal of the American Society for Mass Spectrometry}
}
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