The Raman spectrum of a protein or nucleic acid consists of numerous discrete bands representing molecular normal modes of vibration and serves as a sensitive and selective fingerprint of three-dimensional structure, intermolecular interactions, and dynamics. Recent improvements in instrumentation, coupled with innovative approaches in experimental design, dramatically increase the power and scope of the method, particularly for investigations of large supramolecular assemblies. Applications are considered that involve the use of () time-resolved Raman spectroscopy to elucidate assembly pathways in icosahedral viruses, () polarized Raman microspectroscopy to determine detailed structural parameters in filamentous viruses, () ultraviolet-resonance Raman spectroscopy to probe selective DNA and protein residues in nucleoprotein complexes, and () difference Raman methods to understand mechanisms of protein/DNA recognition in gene regulatory and chromosomal complexes.


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  • Article Type: Review Article
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