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dc.creatorLeavitt, Christopher M.en_US
dc.creatorWolk, Arron B.en_US
dc.creatorKamrath, Michael Z.en_US
dc.creatorGarand, Etienneen_US
dc.creatorJohnson, Mark A.en_US
dc.creatorStipdonk, Michael J. Vanen_US
dc.date.accessioned2011-07-12T17:27:58Z
dc.date.available2011-07-12T17:27:58Z
dc.date.issued2011en_US
dc.identifier2011-RG-01en_US
dc.identifier.urihttp://hdl.handle.net/1811/49342
dc.descriptionAuthor Institution: Sterling Chemistry Laboratory, Yale University, PO Box 208107, New Haven, CT 06520; Department of Chemistry, Wichita State University, 1845 Fairmont Ave, Wichita, KS 67208en_US
dc.description.abstractH$_2$ predissociation spectroscopy was used to collect the vibrational spectra of the model protonated peptides, GlyGly, GlySar, SarGly and SarSar (Gly=glycine and Sar=sarcosine). H$_2$ molecules were condensed onto protonated peptide ions in a quadrupole ion trap cooled to approximately 10 K. The resulting spectra yielded clearly resolved vibrational transitions throughout the mid IR region, 600-4200 cm$^{-1}$, with linewidths of approximately 6 cm$^{-1}$. Protonation nominally occurred on the amino terminus giving rise to an intramolecular H-bond between the protonated amine and the neighboring amide oxygen. The sarcosine containing peptides incorporate a methyl group onto either the amino group or the amide nitrogen causing the peptide backbone to adopt a different structure, resulting in the shifts in the amide I and II bands and the N-H stretches.en_US
dc.language.isoenen_US
dc.publisherOhio State Universityen_US
dc.titleVIBRATIONAL SPECTRA OF CRYOGENIC PEPTIDE IONS USING H$_2$ PREDISSOCIATION SPECTROSCOPYen_US
dc.typeArticleen_US
dc.typeImageen_US
dc.typePresentationen_US


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