The Raman spectrum of a protein or nucleic acid consists of numerous discre
te bands representing molecular normal modes of vibration and serves as a s
ensitive and selective fingerprint of three-dimensional structure, intermol
ecular interactions, and dynamics. Recent improvements in instrumentation,
coupled with innovative approaches in experimental design, dramatically inc
rease the power and scope of the method, particularly for investigations of
large supramolecular assemblies. Applications are considered that involve
the use of (a) time-resolved Raman spectroscopy to elucidate assembly pathw
ays in icosahedral viruses, (b) polarized Raman microspectroscopy to determ
ine detailed structural parameters in filamentous viruses, (c) ultraviolet-
resonance Raman spectroscopy to probe selective DNA and protein residues in
nucleoprotein complexes, and (d) difference Raman methods to understand me
chanisms of protein/DNA recognition in gene regulatory and chromosomal comp
lexes.