title: Single-conformation infrared spectra of model peptides in the amide I and amide II regions: experiment-based determination of local mode frequencies and inter-mode coupling.
abstract: Single-conformation infrared spectra in the amide I and amide II regions have been recorded for a total of 34 conformations of three α-peptides, three β-peptides, four α/β-peptides, and one γ-peptide using resonant ion-dip infrared spectroscopy of the jet-cooled, isolated molecules. Assignments based on the amide NH stretch region were in hand, with the amide I/II data providing additional evidence in favor of the assignments. A set of 21 conformations that represent the full range of H-bonded structures were chosen to characterize the conformational dependence of the vibrational frequencies and infrared intensities of the local amide I and amide II modes and their amide I/I and amide II/II coupling constants. Scaled, harmonic calculations at the DFT M05-2X/6-31+G(d) level of theory accurately reproduce the experimental frequencies and infrared intensities in both the amide I and amide II regions. In the amide I region, Hessian reconstruction was used to extract local mode frequencies and amide I/I coupling constants for each conformation. These local amide I frequencies are in excellent agreement with those predicted by DFT calculations on the corresponding (13)C = (18)O isotopologues. In the amide II region, potential energy distribution analysis was combined with the Hessian reconstruction scheme to extract local amide II frequencies and amide II/II coupling constants. The agreement between these local amide II frequencies and those obtained from DFT calculations on the N-D isotopologues is slightly worse than for the corresponding comparison in the amide I region. The local mode frequencies in both regions are dictated by a combination of the direct H-bonding environment and indirect, "backside" H-bonds to the same amide group. More importantly, the sign and magnitude of the inter-amide coupling constants in both the amide I and amide II regions is shown to be characteristic of the size of the H-bonded ring linking the two amide groups. These amide I/I and amide II/II coupling constants remain similar in size for α-, β-, and γ-peptides despite the increasing number of C-C bonds separating the amide groups. These findings provide a simple, unifying picture for future attempts to base the calculation of both nearest-neighbor and next-nearest-neighbor coupling constants on a joint footing.
authors.affiliation: Department of Chemistry, Purdue University, West Lafayette, Indiana 47907-2084, USA.
authors.forename: Evan G
authors.initials: EG
authors.lastname: Buchanan
authors.forename: William H
authors.initials: WH
authors.lastname: James
authors.forename: Soo Hyuk
authors.initials: SH
authors.lastname: Choi
authors.forename: Li
authors.initials: L
authors.lastname: Guo
authors.forename: Samuel H
authors.initials: SH
authors.lastname: Gellman
authors.forename: Christian W
authors.initials: CW
authors.lastname: Müller
authors.forename: Timothy S
authors.initials: TS
authors.lastname: Zwier
mesh_terms: D000577:Amides / Q000737:chemistry*; D008958:Models, Molecular; D009842:Oligopeptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D011789:Quantum Theory; D013055:Spectrophotometry, Infrared
chemical_list: D000577:Amides; D009842:Oligopeptides