UNIT 17.8 Raman Spectroscopy of Proteins and Nucleoproteins

  1. Daniel Nemecek1,4,
  2. Josef Stepanek2,
  3. George J. Thomas Jr.3

Published Online: 1 FEB 2013

DOI: 10.1002/0471140864.ps1708s71

Current Protocols in Protein Science

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.

Author Information

  1. 1

    National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland

  2. 2

    Charles University in Prague, Faculty of Mathematics and Physics, Institute of Physics, Prague, Czech Republic

  3. 3

    School of Biological Sciences, University of Missouri-Kansas City, Kansas City, Missouri

  4. 4

    Central European Institute of Technology, Masaryk University , Brno, Czech Republic

Publication History

  1. Published Online: 1 FEB 2013
  2. 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