화학공학소재연구정보센터
Journal of Physical Chemistry B, Vol.108, No.46, 18034-18045, 2004
Peptide secondary structure determination by three-pulse coherent vibrational spectroscopies: A simulation study
Amide I mode vibrational spectra of four ideal secondary structural motiffs of peptides, alpha helix, 3(10) helix, parallel beta sheet, and antiparallel beta sheet, in response to three infrared pulses with wavevectors k(1), k(2), and k(3) are simulated using a vibrational exciton model. Correlation plots of the signals generated at -k(1) + k(2) + k(3) and +k(1) + k(2) - k(3) show a characteristic peak pattern for each motiff. Resolution is enhanced by applying specific polarization configurations of the optical fields to oriented peptides.