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Chapter E1 - Visible and IR absorption spectroscopy

from Part E - Optical spectroscopy

Published online by Cambridge University Press:  05 November 2012

Igor N. Serdyuk ,
Nathan R. Zaccai  and
Joseph Zaccai
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

Brief historical review and biological applications

1704

In OpticksIsaac Newton dealt with the formation of a spectrum by a prism, and the composition of white light and its dispersion. The Latin word, spectrum, means an appearance; a spectrum is obtained when radiation is broken up into its colour or wavelength distribution.

1800

The astronomer, William Herschel, discovered infrared (IR) radiation.

1801

The physicist Johann Wilhelm Ritter discovered ultraviolet (UV) radia-tion.

1814

Joseph von Frauenhofer showed that the Sun's spectrum contained dark lines (later named Frauenhofer lines), indicating that light of the corresponding colour was missing because of absorption.

1850–1900

August Beer stated the empirical law, which was named after him, that there is an exponential dependence between the transmision of light through a substance, the concentration of the substance and the path length of the beam through it. The law is also known as the Beer–Lambert law or the Beer–Lambert–Bouguer law, in recognition of the work of Pierre Bouguer (1729) and Johann Heinrich Lambert (1760). Gustav Kirchhoff's discovery that each pure substance has a characteristic spectrum provided the basis for analytical spectroscopy. Gustav Kirchhoff and Robert Bunsen identified the chemical elements in the Sun by analysing its spectrum. Johann Jacob Balmer identified a numerical series in the spectrum of hydrogen. Joseph John Thomson discovered the electron. Max Planck introduced the concept of quanta in the treatment of heat radiation and laid the foundation of quantum theory. He was awarded the Nobel prize in 1918.

Type
Chapter
Information
Methods in Molecular Biophysics
Structure, Dynamics, Function
 , pp. 519 - 561
Publisher: Cambridge University Press
Print publication year: 2007

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References

Seibert, F. B. (1995). Infrared spectroscopy applied to biochemical and biological problems. Meth. Enzymol., 246, 501–526.CrossRefGoogle Scholar
Chalmers, J. M., and Griffiths, P. R. (eds.) (2002). Handbook of Vibrational Spectroscopy, 5 volumes. Chichester: John Wiley and Sons Ltd.Google Scholar
Gauglitz, G., and Vo-Dinh, T. (eds.) (2003). Handbook of Spectroscopy, 2 volumes. Weinheim: Wiley-VCH Verlag GmbH KgaA.CrossRefGoogle Scholar
Jakson, M., Sowa, M. G., and Mantsch, H. H. (1997). Infrared spectroscopy: a new frontier in medicine. Biophys. Chem., 68, 109–125.CrossRefGoogle Scholar
Tinoco, I. Jr. (1995). Optical spectroscopy: General principles and overview. Meth. Enzymol., 246, 13–18.CrossRefGoogle Scholar
Taillandier, E., Firon, M., and Liquier, J. (1991). In Spectroscopy of Biological Macromolecules, eds. Hester, R. E. and Girling, R. B.. Cambridge: Royal Society of Chemistry.Google Scholar
Mathies, R. (1995). Biomolecular vibrational spectroscopy. Meth. Enzymol., 246, 377–389.CrossRefGoogle ScholarPubMed
Sauer, K. (1995). Why spectroscopy? Which spectroscopy? Meth. Enzymol., 246, 1–10.CrossRefGoogle Scholar
Tinoco, I. Jr, Sauer, K., and Wang, J. C. (1998). Molecular structure and interactions: physical chemistry. In Principles and Applications in Biological Science. Ch. 10. Molecular structures and interactions: Spectroscopy. Upper Saddle River, NJ: Prentice Hall.Google Scholar
Miura, T., and Thomas, G. J. Jr, (1995). Optical and vibrational spectroscopic methods. In Introduction to Biophysical Methods for Protein and Nucleic Acid Research, eds. Glasel, J. A. and Deutcher, M. P.. London: Academic Press.Google Scholar
Miyazawa, T., and Blout, E. R. (1961). The infrared spectra of polypeptides in various conformations: Amide I and II bands. JACS, 83, 712–719.CrossRefGoogle Scholar
Heberle, J., and Gensch, Th. (2001). When FT-IR spectroscopy meets X-ray crystallography. Nature Struct. Biol., 8, 195–197.CrossRefGoogle ScholarPubMed
Surevicz, W. K., Mantsch, H. H., and Chapman, D. (1993). Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment. Biochemistry, 32, 389–394.CrossRefGoogle Scholar
Susi, H., and Byler, D. M. (1986). Resolution-enhanced Fourier transform infrared spectroscopy of enzymes. Meth. Enzymol. 130, 290–311.CrossRefGoogle ScholarPubMed
Braiman, M. S., and Rotschild, K. J. (1988). Fourier transform infrared techniques for probing membrane protein structure. Ann. Rev. Biophys. Chem., 17, 541–570.CrossRefGoogle ScholarPubMed
Bandecar, J. (1992). Amide modes and protein conformation. Biochim. Biophys. Acta. 1120, 123–143.CrossRefGoogle Scholar
Arrondo, J. L. R., Muga, A., Castresana, J., and Goni, F. M. (1993). Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy. Progr. Biophys. Mol. Biol., 59, 23–56.CrossRefGoogle ScholarPubMed
Mantele, W. (1993). Reaction-induced infrared difference spectroscopy for the study of protein function and reaction mechanisms. TIBS, 18, 197–202.Google Scholar
Martin, J-L., and Vos, M. H. (1992). Femtosecond biology. Annu. Rev. Biophys. Biomol. Struct., 21, 199–222.CrossRefGoogle ScholarPubMed
Gevert, K. (1993). Molecular reaction mechanisms of proteins as monitored by time-resolved FTIR spectroscopy. Curr. Opin. Struct. Biol., 3, 769–773.Google Scholar
Taillandier, E., and Liquier, J. (1992). Infrared spectroscopy of DNA. Meth. Enzymol., 211, 307–352.CrossRefGoogle ScholarPubMed
Seibert, F. B. (1995). Infrared spectroscopy applied to biochemical and biological problems. Meth. Enzymol., 246, 501–526.CrossRefGoogle Scholar
Chalmers, J. M., and Griffiths, P. R. (eds.) (2002). Handbook of Vibrational Spectroscopy, 5 volumes. Chichester: John Wiley and Sons Ltd.Google Scholar
Gauglitz, G., and Vo-Dinh, T. (eds.) (2003). Handbook of Spectroscopy, 2 volumes. Weinheim: Wiley-VCH Verlag GmbH KgaA.CrossRefGoogle Scholar
Jakson, M., Sowa, M. G., and Mantsch, H. H. (1997). Infrared spectroscopy: a new frontier in medicine. Biophys. Chem., 68, 109–125.CrossRefGoogle Scholar
Tinoco, I. Jr. (1995). Optical spectroscopy: General principles and overview. Meth. Enzymol., 246, 13–18.CrossRefGoogle Scholar
Taillandier, E., Firon, M., and Liquier, J. (1991). In Spectroscopy of Biological Macromolecules, eds. Hester, R. E. and Girling, R. B.. Cambridge: Royal Society of Chemistry.Google Scholar
Mathies, R. (1995). Biomolecular vibrational spectroscopy. Meth. Enzymol., 246, 377–389.CrossRefGoogle ScholarPubMed
Sauer, K. (1995). Why spectroscopy? Which spectroscopy? Meth. Enzymol., 246, 1–10.CrossRefGoogle Scholar
Tinoco, I. Jr, Sauer, K., and Wang, J. C. (1998). Molecular structure and interactions: physical chemistry. In Principles and Applications in Biological Science. Ch. 10. Molecular structures and interactions: Spectroscopy. Upper Saddle River, NJ: Prentice Hall.Google Scholar
Miura, T., and Thomas, G. J. Jr, (1995). Optical and vibrational spectroscopic methods. In Introduction to Biophysical Methods for Protein and Nucleic Acid Research, eds. Glasel, J. A. and Deutcher, M. P.. London: Academic Press.Google Scholar
Miyazawa, T., and Blout, E. R. (1961). The infrared spectra of polypeptides in various conformations: Amide I and II bands. JACS, 83, 712–719.CrossRefGoogle Scholar
Heberle, J., and Gensch, Th. (2001). When FT-IR spectroscopy meets X-ray crystallography. Nature Struct. Biol., 8, 195–197.CrossRefGoogle ScholarPubMed
Surevicz, W. K., Mantsch, H. H., and Chapman, D. (1993). Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment. Biochemistry, 32, 389–394.CrossRefGoogle Scholar
Susi, H., and Byler, D. M. (1986). Resolution-enhanced Fourier transform infrared spectroscopy of enzymes. Meth. Enzymol. 130, 290–311.CrossRefGoogle ScholarPubMed
Braiman, M. S., and Rotschild, K. J. (1988). Fourier transform infrared techniques for probing membrane protein structure. Ann. Rev. Biophys. Chem., 17, 541–570.CrossRefGoogle ScholarPubMed
Bandecar, J. (1992). Amide modes and protein conformation. Biochim. Biophys. Acta. 1120, 123–143.CrossRefGoogle Scholar
Arrondo, J. L. R., Muga, A., Castresana, J., and Goni, F. M. (1993). Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy. Progr. Biophys. Mol. Biol., 59, 23–56.CrossRefGoogle ScholarPubMed
Mantele, W. (1993). Reaction-induced infrared difference spectroscopy for the study of protein function and reaction mechanisms. TIBS, 18, 197–202.Google Scholar
Martin, J-L., and Vos, M. H. (1992). Femtosecond biology. Annu. Rev. Biophys. Biomol. Struct., 21, 199–222.CrossRefGoogle ScholarPubMed
Gevert, K. (1993). Molecular reaction mechanisms of proteins as monitored by time-resolved FTIR spectroscopy. Curr. Opin. Struct. Biol., 3, 769–773.Google Scholar
Taillandier, E., and Liquier, J. (1992). Infrared spectroscopy of DNA. Meth. Enzymol., 211, 307–352.CrossRefGoogle ScholarPubMed

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