UNIT 17.8 Raman Spectroscopy of Proteins and Nucleoproteins
Published Online: 1 FEB 2013
Copyright © 2013 by John Wiley & Sons, Inc.
Lab Protocol Title
Current Protocols in Protein Science
How to Cite
Nemecek, D., Stepanek, J. and Thomas, G. J. 2013. Raman Spectroscopy of Proteins and Nucleoproteins. Current Protocols in Protein Science. 71:17.8:17.8.1–17.8.52.
- Published Online: 1 FEB 2013
- Published Print: FEB 2013
A protein Raman spectrum comprises discrete bands representing vibrational modes of the peptide backbone and its side chains. The spectral positions, intensities, and polarizations of the Raman bands are sensitive to protein secondary, tertiary, and quaternary structures and to side-chain orientations and local environments. In favorable cases, the Raman spectrum serves as an empirical signature of protein three-dimensional structure, intramolecular dynamics, and intermolecular interactions. Quantitative analysis of Raman spectral series can be further boosted by advanced statistical approaches of factor analysis that allow fitting of specific theoretical models while reducing the amount of analyzed data. Here, the strengths of Raman spectroscopy are illustrated by considering recent applications from the authors' work that address (1) subunit folding and recognition in assembly of the icosahedral bacteriophages, (2) orientations of subunit main chains and side chains in native filamentous viruses, (3) roles of cysteine hydrogen bonding in the folding, assembly, and function of virus structural proteins, and (4) structural determinants of protein/DNA recognition in gene regulatory complexes. Conventional Raman and polarized Raman techniques are surveyed. Curr. Protoc. Protein Sci. 71:17.8.1-17.8.52. © 2013 by John Wiley & Sons, Inc.
- viral protein;
- virus assembly;
- DNA recognition;
- Raman spectroscopy;
- polarized Raman spectroscopy