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Updated: Jun 18, 2026

Submillisecond Conformational Changes in Proteins Resolved by Photothermal Beam Deflection
Published on: February 18, 2014
Signatures of beta-peptide unfolding in two-dimensional vibrational echo spectroscopy: a simulation study
C Scheurer1, A Piryatinski, S Mukamel
1Department of Chemistry, University of Rochester, Rochester, New York 14627, USA. chris@feynman.chem.rochester.edu
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.
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