作者: Sander Woutersen , Peter Hamm
DOI: 10.1063/1.1407842
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摘要: Nonlinear two-dimensional (2D) vibrational spectroscopy has been used to investigate the amide I band of an alanine-based 21-residue α-helical peptide in aqueous solution. Whereas linear absorption spectrum consists a single, broad band, 2D clearly reveals that this is composed two transitions, which are assigned A and E1 modes. The A–E1 frequency splitting found be approximately 10 cm−1. We find inhomogeneously broadened due conformational disorder helix. line shapes can well described using distributions dihedral angles (φ,ψ) around their average values with width 20°, confirming previous molecular-dynamics studies. Time-resolved measurements show conformation fluctuates on time scale picoseconds.