title: Single-conformation ultraviolet and infrared spectroscopy of model synthetic foldamers: beta-peptides Ac-beta3-hPhe-NHMe and Ac-beta3-hTyr-NHMe.
abstract: The conformational preferences and infrared and ultraviolet spectral signatures of two model beta-peptides, Ac-beta3-hPhe-NHMe (1) and Ac-beta3-hTyr-NHMe (2), have been explored under jet-cooled, isolated molecule conditions. The mass-resolved, resonant two-photon ionization spectra of the two molecules were recorded in the region of the S0-S1 origin of the phenyl or phenol ring substituents, respectively. UV-UV hole-burning spectroscopy was used to determine that two conformations of 1 are present, with the transitions due to conformer A, with S0-S1 origin at 34431 cm(-1), being almost 20 times larger than those due to conformer B, with S0-S1 origin at 34404 cm(-1). Only one conformation of 2 was observed. Resonant ion-dip infrared spectroscopy provided single-conformation infrared spectra in the 3300-3700 cm(-1) region. The spectra of conformer A of both molecules have H-bonded and free amide NH stretch infrared transitions at 3400 and 3488 cm(-1), respectively, while conformer B of 1 possesses bands at 3417 and 3454 cm(-1). For comparison with experiment, full optimizations of all low-lying minima of 1 were carried out at the DFT B3LYP/6-31+G* and RIMP2/aug-cc-pVDZ levels of theory, and single point MP2/6-31+G* calculations at the DFT geometries. On the basis of the comparison with previous studies in solution and the calculated results, conformer A of 1 and 2 were assigned to a C6 conformer, while conformer B of 1 was assigned to a unique C8 structure with a weak intramolecular H-bond. The reasons for the preference for C6 over C8 structures and the presence of only two conformations in the jet-cooled spectrum are discussed in light of the predictions from calculations.
authors.affiliation: Department of Chemistry, Purdue University, West Lafayette, Indiana 49707-2084, USA.
authors.forename: Esteban E
authors.initials: EE
authors.lastname: Baquero
authors.forename: William H
authors.initials: WH
authors.lastname: James
authors.forename: Soo Hyuk
authors.initials: SH
authors.lastname: Choi
authors.forename: Samuel H
authors.initials: SH
authors.lastname: Gellman
authors.forename: Timothy S
authors.initials: TS
authors.lastname: Zwier
mesh_terms: D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D010649:Phenylalanine / Q000031:analogs & derivatives; D011487:Protein Conformation; D017510:Protein Folding; D013055:Spectrophotometry, Infrared; D013056:Spectrophotometry, Ultraviolet; D013816:Thermodynamics; D014443:Tyrosine / Q000031:analogs & derivatives
chemical_list: D010455:Peptides; D014443:Tyrosine; D010649:Phenylalanine