title: Signatures of beta-peptide unfolding in two-dimensional vibrational echo spectroscopy: a simulation study.
abstract: An ensemble of exciton Hamiltonians for the amide-I band of the folded and unfolded states of a helical beta-heptapeptide is generated using a molecular dynamics (MD) simulation. The correlated fluctuations of its parameters and their signatures in two-dimensional (2D) vibrational echo spectroscopy are computed. This technique uses infrared pulse sequences to provide ultrafast snapshots of molecular structural fluctuations, in analogy with multidimensional NMR. The present study demonstrates that, by combining a method of calculating the vibrational Hamiltonian from MD snapshots and the nonlinear exciton equations (NEE), it may be possible to simulate realistic multidimensional IR spectra of chemically and biologically interesting systems.
authors.affiliation: Department of Chemistry, University of Rochester, Rochester, New York 14627, USA. chris@feynman.chem.rochester.edu
authors.forename: C
authors.initials: C
authors.lastname: Scheurer
authors.forename: A
authors.initials: A
authors.lastname: Piryatinski
authors.forename: S
authors.initials: S
authors.lastname: Mukamel
mesh_terms: D003198:Computer Simulation; D008956:Models, Chemical; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding; D013055:Spectrophotometry, Infrared / Q000379:methods*; D013816:Thermodynamics
chemical_list: D010455:Peptides