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Chapter E3 - Raman scattering spectroscopy

from Part E - Optical spectroscopy

Published online by Cambridge University Press:  05 November 2012

Igor N. Serdyuk
Affiliation:
Institute of Protein Research, Moscow
Nathan R. Zaccai
Affiliation:
University of Bristol
Joseph Zaccai
Affiliation:
Institut de Biologie Structurale, Grenoble
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Summary

Historical review and introduction to biological problems

1928

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.

Type
Chapter
Information
Methods in Molecular Biophysics
Structure, Dynamics, Function
, pp. 573 - 600
Publisher: Cambridge University Press
Print publication year: 2007

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References

Cary, P. R. (1982). Biochemical Applications of Raman and Resonance Raman Spectroscopy. London: Academic Press.Google Scholar
Asher, S. A. (1993). UV resonance Raman spectroscopy for analytical, physical, and biophysical chemistry. Part I. Analyt. Chem., 65, 59A–66A.CrossRefGoogle Scholar
Asher, S. A. (1993). UV resonance Raman spectroscopy for analytical, physical, and biophysical chemistry. Part II. Analyt. Chem., 65, 201A–210A.CrossRefGoogle ScholarPubMed
Tomas, G. J. Jr (1999). Raman spectroscopy of protein and nucleic acid assemblies. Annu. Rev. Biophys. Biomol. Struct., 28, 1–27.CrossRefGoogle Scholar
Skoog, D. A., Holler, F. J., and Nieman, T. A. (1995). Principle of Instrumental Analysis, Philadelphia; PA: Saunders College Publishing.Google Scholar
Peticolas, W. L. (1995). Raman spectroscopy of DNA and proteins. Meth. Enzymol., 246, 389–415.CrossRefGoogle ScholarPubMed
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.CrossRefGoogle ScholarPubMed
Williams, R. W. (1986). Protein secondary structure analysis using Raman Amide I and Amide III spectra. Meth. Enzymol., 130, 311–331.CrossRefGoogle ScholarPubMed
Hudson, B., and Mayne, L. (1986). Ultraviolet resonance Raman spectroscopy in biopolymers. Meth. Enzymol., 130, 331–350.CrossRefGoogle ScholarPubMed
Spiro, T. G., and Chernuszevich, R. S. (1995). Resonance Raman spectroscopy of metalloprotein. Meth. Enzymol., 246, 416–459.CrossRefGoogle Scholar
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.CrossRefGoogle ScholarPubMed
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.CrossRefGoogle ScholarPubMed
Kincaid, J. (1995). Structure and dynamics of transient species using time-resolved Resonance Raman spectroscopy. Meth. Enzymol., 246, 461–501.Google ScholarPubMed
Cary, P. R. (1982). Biochemical Applications of Raman and Resonance Raman Spectroscopy. London: Academic Press.Google Scholar
Asher, S. A. (1993). UV resonance Raman spectroscopy for analytical, physical, and biophysical chemistry. Part I. Analyt. Chem., 65, 59A–66A.CrossRefGoogle Scholar
Asher, S. A. (1993). UV resonance Raman spectroscopy for analytical, physical, and biophysical chemistry. Part II. Analyt. Chem., 65, 201A–210A.CrossRefGoogle ScholarPubMed
Tomas, G. J. Jr (1999). Raman spectroscopy of protein and nucleic acid assemblies. Annu. Rev. Biophys. Biomol. Struct., 28, 1–27.CrossRefGoogle Scholar
Skoog, D. A., Holler, F. J., and Nieman, T. A. (1995). Principle of Instrumental Analysis, Philadelphia; PA: Saunders College Publishing.Google Scholar
Peticolas, W. L. (1995). Raman spectroscopy of DNA and proteins. Meth. Enzymol., 246, 389–415.CrossRefGoogle ScholarPubMed
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.CrossRefGoogle ScholarPubMed
Williams, R. W. (1986). Protein secondary structure analysis using Raman Amide I and Amide III spectra. Meth. Enzymol., 130, 311–331.CrossRefGoogle ScholarPubMed
Hudson, B., and Mayne, L. (1986). Ultraviolet resonance Raman spectroscopy in biopolymers. Meth. Enzymol., 130, 331–350.CrossRefGoogle ScholarPubMed
Spiro, T. G., and Chernuszevich, R. S. (1995). Resonance Raman spectroscopy of metalloprotein. Meth. Enzymol., 246, 416–459.CrossRefGoogle Scholar
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.CrossRefGoogle ScholarPubMed
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.CrossRefGoogle ScholarPubMed
Kincaid, J. (1995). Structure and dynamics of transient species using time-resolved Resonance Raman spectroscopy. Meth. Enzymol., 246, 461–501.Google ScholarPubMed

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