Ultraviolet resonance Raman (UVRR) spectra of H 2 O and D 2 O solutions of the nucleoside (dA, dG, dC, dT) and aromatic amino acid (Phe, Trp, Tyr) constituents of DNA viruses have been obtained with laser excitation wavelengths of 257, 244, 238, and 229 nm. Using the 981 cm 01 marker of Na 2 SO 4 as
Structural studies of viruses by Raman spectroscopy. Novel vibrational assignments for proteins from Raman spectra of viruses
✍ Scribed by Stacy A. Overman; George J. Thomas Jr
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 303 KB
- Volume
- 29
- Category
- Article
- ISSN
- 0377-0486
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✦ Synopsis
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 compoundÏ and its Raman signature may provide novel spectrastructure 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 Ðlamentous viruses are identiÐed. The Raman bands in question have not been identiÐed previously in proteins and are demonstrated to originate either from vibrations of the protein main-chain (CaH 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 signiÐcance of protein Raman bands.
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