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  • Print publication year: 2007
  • Online publication date: November 2012

Chapter E3 - Raman scattering spectroscopy

from Part E - Optical spectroscopy


Historical review and introduction to biological problems


L. Mandelshtam and C. V. Raman independently discovered that a wavelength shift in a small fraction of scattered visible radiation depends on the chemical structure of the molecule responsible for the scattering. Raman was awarded the 1931 Nobel Prize in physics for the discovery of the phenomenon, which became known as Raman scattering or the Raman effect (Comment E3.1).

Comment E3.1

Mandelshtam–Raman phenomenon

In Russian scientific literature the effect is called the Mandelshtam–Raman phenomenon. We follow the more general usage and call it the Raman effect.

Raman scattering is inelastic light scattering that results from the same type of quantised vibrational transitions as those associated with IR absorption and occurs in the same spectral region. The Raman scattering and IR absorption spectra for a given molecule are often similar. Differences between the properties that make a chemical group IR or Raman active, however, make the techniques strongly complementary rather than competitive. Raman spectroscopy has the advantages of minimal or no damage to the sample, and relatively little interference from the water signal in aqueous solution or in vivo. The possibility of observing Raman spectra from crystals as well as from solutions in vitro or in vivo provides a very useful approach to relating molecular structures solved by X-ray crystallography and conformations in solution or in living cells.

Raman spectroscopy was not widely used by molecular biophysicists until lasers became available in the 1960s.

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Suggestions for further reading
Historical review and introduction to biological problems
Cary, P. R. (1982). Biochemical Applications of Raman and Resonance Raman Spectroscopy. London: Academic Press.
Asher, S. A. (1993). UV resonance Raman spectroscopy for analytical, physical, and biophysical chemistry. Part I. Analyt. Chem., 65, 59A–66A.
Asher, S. A. (1993). UV resonance Raman spectroscopy for analytical, physical, and biophysical chemistry. Part II. Analyt. Chem., 65, 201A–210A.
Non-resonance Raman spectroscopy
Tomas, G. J. Jr (1999). Raman spectroscopy of protein and nucleic acid assemblies. Annu. Rev. Biophys. Biomol. Struct., 28, 1–27.
Skoog, D. A., Holler, F. J., and Nieman, T. A. (1995). Principle of Instrumental Analysis, Philadelphia; PA: Saunders College Publishing.
Peticolas, W. L. (1995). Raman spectroscopy of DNA and proteins. Meth. Enzymol., 246, 389–415.
Callender, R., and Deng, H. (1994). Nonresonance Raman difference spectroscopy: a general probe of protein structure, ligand binding, enzymatic catalysis, and the structures of other biomacromolecules. Annu. Rev. Biophys. Biomol. Struct., 23, 215–245.
Williams, R. W. (1986). Protein secondary structure analysis using Raman Amide I and Amide III spectra. Meth. Enzymol., 130, 311–331.
Resonance Raman spectroscopy
Hudson, B., and Mayne, L. (1986). Ultraviolet resonance Raman spectroscopy in biopolymers. Meth. Enzymol., 130, 331–350.
Spiro, T. G., and Chernuszevich, R. S. (1995). Resonance Raman spectroscopy of metalloprotein. Meth. Enzymol., 246, 416–459.
Vibrational Raman optical activity
Barron, L. D., Hecht, L., Blanch, E. W., and Bell, A. F. (2000). Solution structure and dynamics of molecules from Raman optical activity. Prog. Biophys. Mol. Biol., 73, 1–49.
Differential Raman spectroscopy
Zheng, R., Zheng, X., Dong, J., and Carey, P. R. (2004). Proteins can convert to β-sheet in single crystals. Protein Sci., 13, 1288–1294.
Time-resolved resonance Raman spectroscopy
Kincaid, J. (1995). Structure and dynamics of transient species using time-resolved Resonance Raman spectroscopy. Meth. Enzymol., 246, 461–501.