Biology – Quantitative Biology – Biomolecules
Scientific paper
Jun 2010
adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=2010mss..confetb07j&link_type=abstract
"International Symposium On Molecular Spectroscopy, 65th Meeting, Held 21-25 June, 2010 at Ohio State University. http://molspec
Biology
Quantitative Biology
Biomolecules
Mini-Symposium: Biomolecules And Cluster Ions
Scientific paper
IR/UV double-resonance spectroscopy has been used to study the intrinsic conformational preferences of naturally occurring and synthetic peptides. These studies demonstrated the power of double-resonance methods and highlighted the ability of even short peptide mimics to form a variety of intramolecular hydrogen bonded architectures. Currently, we are extending these studies to a series of model γ2-peptides, which differ from α-peptides by virtue of having two additional, substitutable methylene units separating amide groups in the peptide backbone. Initial studies centered on the conformation-specific infrared spectra of Ac-γ2-hPhe-NHMe, where three unique conformational isomers (two hydrogen-bonded and one intramolecular amide stacked) were observed under the isolated-molecule conditions of a jet-cooled environment. This talk will focus on on two larger γ2-peptides, Ac-γ2-hPhe-γ2-hAla-NHMe and Ac-γ2-hAla-γ2-hPhe-NHMe. Utilizing resonant ion-dip infrared spectroscopy, the single-conformation infrared spectra of eight resolved conformers of the two molecules were recorded in the amide NH stretch region. The resulting infrared spectra of the tri-amides contain evidence for structures comprised of one, two, and three intramolecular amide-amide hydrogen bonds, the last of which is unprecedented for a tri-amide. In an effort to make firm conformational assignments, the spectroscopic data will be compared to the results of harmonic vibrational frequency calculations using traditional DFT and dispersion-corrected DFT methods, the results of which will be discussed.
Buchanan Evan G.
Gellman Samuel H.
Guo Li
James William H. III
Müller Christian W.
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