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Raman spectroscopy and ultraviolet resonance Raman spectroscopy are versatile methods for probing details of protein structure and dynamics in complex biological assemblies, including viruses. The information contained in the Raman spectrum of a virus is ordinarily interpreted on the basis of an understanding that has been developed from detailed spectroscopic investigations of simpler and better characterized molecular structures, such as small globular proteins, peptides and related model compounds and their isotopic derivatives. The model systems approach serves generally as the foundation for reliable band assignments and has been the key to successful application of Raman methods to supramolecular assemblies. However, the converse approach is also possible. The supramolecular assembly may serve as a ‘model compound’ and its Raman signature may provide novel spectra–structure correlations applicable to isolated protein subunits, simpler proteins or related small molecules. Thus, the Raman spectrum of a virus particle can yield new insights into protein vibrational assignments. Here, a number of new vibrational assignments that have emerged from Raman studies of filamentous viruses are identified. The Raman bands in question have not been identified previously in proteins and are demonstrated to originate either from vibrations of the protein main-chain (CαH marker, 1340–1350 cm-1) or from aromatic amino acid side chains (phenylalanine marker, 827 cm-1; tyrosine singlet, 850–855 cm-1; tryptophan marker, 1560 cm-1). The present results, which are considered in the light of existing correlations between data on Raman spectra and protein structure, suggest that much remains to be learned about the structural significance of protein Raman bands. © 1998 John Wiley & Sons, Ltd.
Overman et al. (Thu,) studied this question.