Add time:08/22/2019 Source:sciencedirect.com
Disulfide bridges are important structural elements in proteins. It is well-known that the position of the characteristic disulfide band at ca. 500 cm−1 in the vibrational spectra varies with the conformation around the disulfide unit. In our computational study on the model system diethyl disulfide, both wavenumber and normal mode composition are analyzed simultaneously as a function of conformation. For the disulfide band, a negative correlation between the calculated vibrational wavenumber and the SS stretching contribution is detected. This trend in the normal mode composition provides an explanation for experimentally observed wavenumber shifts of the disulfide band.
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