Vibrational Characterization of Simple Peptides Using Cryogenic Infrared Photodissociation of H2-TAGGED, Mass-Selected Ions

Details Vibrational Characterization of Simple Peptides Using Cryogenic Infrared Photodissociation of H2-TAGGED, Mass-Selected Ions Vibrational Characterization of Simple Peptides Using Cryogenic Infrared Photodissociation of H2-TAGGED, Mass-Selected Ions

Jun 2011

adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=2011mss..conferg02k&link_type=abstract

"International Symposium On Molecular Spectroscopy, 66th Meeting, Held 20-24 June, 2011 at Ohio State University. http://molspec

Computer Science

Infrared/Raman

Scientific paper

We present infrared photodissociation spectra of two protonated peptides that are cooled in a 10 K quadrupole ion trap and "tagged" with weakly bound H2 molecules. Spectra are recorded over the range 600 - 4300 Cm-1 using a table-top laser source, and are shown to result from one-photon absorption events. This arrangement is demonstrated to recover sharp (Δ ν = 6 Cm-1) transitions throughout the fingerprint region, despite the very high density of vibrational states in this energy range. The fundamentals associated with all of the signature N-H and C=O stretching bands are completely resolved. To address the site-specificity of the C=O stretches near 1800 Cm-1, we incorporated one 13C into the tripeptide. The labeling affects only one line in the complex spectrum, indicating that each C=O oscillator contributes a single distinct band, effectively "reporting" its local chemical environment. For both peptides, analysis of the resulting band patterns indicates that only one isomeric form is generated upon cooling the ions initially at room temperature into the H2 tagging regime.

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