Disentangling Peptide Configurations via Two-Dimensional Electronic Spectroscopy: Ab Initio Simulations Beyond the Frenkel Exciton Hamiltonian.

ABSTRACT: Two-dimensional (2D) optical spectroscopy techniques based on ultrashort laser pulses have been recently extended to the optical domain in the ultraviolet (UV) spectral region. UV-active aromatic side chains can thus be used as local highly specific markers for tracking dynamics and structural rearrangements of proteins. Here we demonstrate that 2D electronic spectra of a model proteic system, a tetrapeptide with two aromatic side chains, contain enough structural information to distinguish between two different configurations with distant and vicinal side chains. For accurate simulations of the 2DUV spectra in solution, we combine a quantum mechanics/molecular mechanics approach based on wave function methods, accounting for interchromophores coupling and environmental effects, with nonli

SUBMITTER: Nenov A 

PROVIDER: S-EPMC3985887 | biostudies-literature | 2014 Feb

REPOSITORIES: biostudies-literature