Raman spectroscopy is still a suitable and prominent method for probing the relationship between structure, dynamics and function of biomolecules. In this context, resonance Raman spectroscopy is of particular relevance since it allows the site‐specific investigation of chromophores (aromatic amino acid residues, nucleotides, heme groups) which are directly involved in mechanisms pivotal for the function of the respective molecules. Time‐resolved spectroscopy (Raman and IR) is utilized to explore, e.g., structural changes in heme proteins upon ligand photolysis. Conventional visible Raman is still a useful tool to explore peptides and proteins and to determine the orientation of oriented nucleic acid fibres.
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Reinhard Schweitzer‐Stenner (2005) studied this question.
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