Recent advances in Raman optical activity (ROA) instrumentation are ou
tlined which have enhanced significantly the quality of vibrational RO
A spectra of biopolymers in aqueous solution. Peptides, proteins, carb
ohydrates, glycoproteins, and nucleic acids now provide excellent ROA
spectra which contain detailed information about solution structure. R
OA spectra can be measured just as easily in D2O as in H2O solution, a
nd, as illustrated for bovine serum albumin and concanavalin A, a comp
arison of the two can be highly informative. In addition to signatures
of extended secondary structure, protein ROA spectra also contain sig
natures related to loops and turns which are valuable for studying ter
tiary structure and dynamics, exemplified here by a comparison of the
ROA spectra of reduced lysozyme and unordered poly-l-lysine, by the RO
A spectra of acid molten globule cu-lactalbumin at different temperatu
res, which reveal a native-like tertiary fold, and by changes in the R
OA spectrum of native lysozyme on binding to a saccharide inhibitor. C
arbohydrate ROA spectra contain signatures of all the central features
of their stereochemistry and, as shown by a comparison of laminaribio
se with laminarin, can also probe extended secondary structure in poly
saccharides. Results on a glycoprotein, orosomucoid, suggest that ROA
can provide information about both the protein and the carbohydrate co
mponents. Preliminary results on nucleic acids are outlined with the R
OA spectra of Poly(rA). Poly(rU) and Poly(rI). Poly(rC) shown as examp
les.