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We review various visible and UV‐resonance Raman experiments on model peptides such as N ‐methylacetamide and di‐ and triglycine which are aimed at exploring the structure and dynamics of these molecules. Whereas visible Raman spectroscopy probes the electronic ground state, the UV Raman technique is utilized additionally to obtain structural information about excited electronic states. This research is aimed at obtaining a spectroscopically determined force field, which can be transferred to polypeptides and proteins. We further argue that the capability of vibrational spectroscopy to probe the structure of peptides and proteins can be significantly improved by combining computational and spectroscopic studies on appropriate model peptides to calibrate wavenumbers and intensities of Raman and IR bands for the quantitative determination of structural parameters such as the dihedral angles.
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Reinhard Schweitzer‐Stenner (2001) studied this question.
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