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Resonance Raman Spectroscopy

  1. Ishita Mukerji

Published Online: 17 DEC 2012

DOI: 10.1002/9780470015902.a0003113.pub2



How to Cite

Mukerji, I. 2012. Resonance Raman Spectroscopy. eLS. .

Author Information

  1. Wesleyan University, Middletown, Connecticut, USA

Publication History

  1. Published Online: 17 DEC 2012


Resonance Raman spectroscopy is a vibrational spectroscopic technique that utilises electronic absorption bands to dramatically enhance the magnitude of the signal. It has been used effectively to study protein structure and function. Resonance Raman spectroscopy performed in the UV spectral range can probe the structure of proteins by monitoring the local environment of aromatic side chains. Deep-UV resonance Raman spectroscopy with excitation wavelengths less than 200 nm can be used to determine secondary structure of proteins by monitoring the frequencies and intensities of amide backbone modes. The ability to monitor both proteins backbone and side chains in kinetic investigations makes this a very powerful technique for investigations of protein folding and amyloid formation.

Key Concepts:

  • Resonance Raman spectroscopy measures molecular vibrations, which provides information on local environment and H-bonding. The resonance effect leads to selective enhancement and a simplified spectrum.

  • Resonance Raman spectroscopy can be used to study samples in a variety of different physical forms such as solutions, gels and fibres.

  • Time-resolved techniques involving resonance Raman spectroscopy span a wide time range from picoseconds to seconds. Selective investigation of chromophores, protein backbones and sidechains provides a wealth of dynamic information.

  • Secondary structure of proteins can be determined using UV resonance Raman spectroscopy, which monitors the amide vibrational modes of the peptide backbone. In particular the amide III3 mode frequency has a sinusoidal dependence on the Ramachandran Ψ angle.

  • UVRR spectroscopy is increasingly being used to study protein folding and the association of proteins and peptides into amyloid fibres.


  • vibrational spectroscopy;
  • proteins;
  • time-resolved;
  • secondary structure conformation;
  • temperature jump