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Chapter D8 - Fluorescence depolarisation

from Part D - Hydrodynamics

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

1926

E. Gaviola created the first instrument for fluorescence measurement, which he called a fluorometer.

1934

F. Perrin formulated the relation between fluorescence depolarisation and Brownian rotary motion for hydrodynamic spherical molecules. In 1936 he extended his treatment to symmetric top molecules.

1952

G. Weber first applied Perrin theory to biological macromolecules. Numerous fluorescence polarisation measurements were carried out under steady-state conditions, utilising constant illumination. Most of them were performed on dye-conjugated macromolecules to determine the harmonic mean rotational relaxation time. Weber's classical review of the application of polarised fluorescence, particularly to proteins, appeared in the 1950s.

1961

A. Jublonski proposed following the rotational relaxation process directly by measuring the decay of the fluorescence polarisation as a function of time. He stressed that time-dependent anisotropy can be interpreted more directly and definitely than its time-average value observed with constant illumination.

1966

P. Wahl, and two years later L. Stryer, experimentally measured the time decay of fluorescence polarisation on dye-conjugated globular proteins.

1969

T. Tao derived relations between the time-dependent fluorescence polarisation anisotropy and the Brownian rotational diffusion coefficients of macromolecules. It was shown that in the most general case of a completely asymmetric body, five exponentials appear in anisotropy. In 1972 analogous results were obtained by other groups (G. G. Belford, R. L. Belford and G. Weber; T. J. Chuang and K. B. Eisenthal).

Type
Chapter
Information
Methods in Molecular Biophysics
Structure, Dynamics, Function
, pp. 446 - 465
Publisher: Cambridge University Press
Print publication year: 2007

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References

Tao, T. (1969). Time dependent fluorescence depolarization and Brownian rotational diffusion coefficients of macromolecules. Biopolymers, 8, 609–632.CrossRefGoogle Scholar
Prendergast, F. G. (1991). Time-resolved fluorescence techniques: methods and application in biology. Curr. Opin. Struct. Biol., 1, 1054–1059.CrossRefGoogle Scholar
Checovich, W. J., Bolger, R. E., and Burke, T. (1995). Fluorescence polarization – a new tool for cell and molecular biology. Nature, 375, 254–256.CrossRefGoogle ScholarPubMed
Weber, G. (1953). Rotational Brownian motion and polarization of the fluorescence of solutions. Adv. Protein Chem., 8, 415–459.CrossRefGoogle ScholarPubMed
Small, E. W., and Isenberg, I. (1977). Hydrodynamic properties of a rigid molecule; rotational and linear diffusion and fluorescence anisotropy. Biopolymers, 16, 1907–1928.CrossRefGoogle ScholarPubMed
Cherry, R. J., and Schneider, G. (1976). A spectroscopic technique for measuring slow rotational diffusion of macromolecules. 2: Determination of rotational correlation times of proteins in solution. Biochemistry, 24, 3657–3661.CrossRefGoogle Scholar
Lakowicz, J. R., Gryczynski, I., et al. (2000). Microsecond dynamics of biological macromolecules. Meth. Enzymol., 323, 473–509.CrossRefGoogle ScholarPubMed
Sportsman, J. R. (2003). Fluorescence anisotropy in pharmacologic screening. Meth. Enzymol., 361, 505–529.CrossRefGoogle ScholarPubMed
Lakowicz, J. R., Gryczynski, I., et al. (2000). Microsecond dynamics of biological macromolecules. Meth. Enzymol., 323, 473–509.CrossRefGoogle ScholarPubMed
Kroes, S. J., Canters, G. W., Giardi, G., Hoek, A., and Visser, A. J. W. G. (1998). Time-resolved fluorescence study of azurin variants: conformational heterogeneity and tryptophan mobility. Biophys. J., 75, 2441–2450.CrossRefGoogle ScholarPubMed
Lakovicz, J. R. (ed.). (1999) Principles of Fluorescence Spectroscopy, second edition. New York: Kluwer Academic/Plenum Publ.CrossRefGoogle Scholar
Cherry, R. J., and Schneider, G. (1976). A spectroscopic technique for measuring slow rotational diffusion of macromolecules. 2: Determination of rotational correlation times of protein in solution. Biochemistry, 15, 3657–3661.CrossRefGoogle Scholar
Ferrer, M. L., Duchowicz, R., Carrasco, B., Garcia de la Torre, J., and Acuna, A. U. (2001). The conformation of serum albumin in solution: a combined phosphorescence depolarization-hydrodynamic modeling study. Biophysical J., 80, 2422–2430.CrossRefGoogle ScholarPubMed
Millar, D. P. (2000). Time-resolved fluorescence methods for analysis of DNA–protein interactions. Meth. Enzymol., 323, 442–459.CrossRefGoogle ScholarPubMed
Hazlett, T. L., Moore, K. J. M., Lowe, P. N., Jameson, D. M., and Eccleston, J. F. (1993). Solution of p21ras proteins bound with fluorescent nucleotides: a time-resolved fluorescence study. Biochemistry, 32, 13575–13583.CrossRefGoogle ScholarPubMed
Canet, D., Doering, K., Dobson, C. M., and Dupont, Y. (2001). High-sensitivity fluorescence anisotropy detection of protein-folding events: Application to α−lactalbumin. Biophys. J., 80, 1996–2003.CrossRefGoogle ScholarPubMed
Tao, T. (1969). Time dependent fluorescence depolarization and Brownian rotational diffusion coefficients of macromolecules. Biopolymers, 8, 609–632.CrossRefGoogle Scholar
Prendergast, F. G. (1991). Time-resolved fluorescence techniques: methods and application in biology. Curr. Opin. Struct. Biol., 1, 1054–1059.CrossRefGoogle Scholar
Checovich, W. J., Bolger, R. E., and Burke, T. (1995). Fluorescence polarization – a new tool for cell and molecular biology. Nature, 375, 254–256.CrossRefGoogle ScholarPubMed
Weber, G. (1953). Rotational Brownian motion and polarization of the fluorescence of solutions. Adv. Protein Chem., 8, 415–459.CrossRefGoogle ScholarPubMed
Small, E. W., and Isenberg, I. (1977). Hydrodynamic properties of a rigid molecule; rotational and linear diffusion and fluorescence anisotropy. Biopolymers, 16, 1907–1928.CrossRefGoogle ScholarPubMed
Cherry, R. J., and Schneider, G. (1976). A spectroscopic technique for measuring slow rotational diffusion of macromolecules. 2: Determination of rotational correlation times of proteins in solution. Biochemistry, 24, 3657–3661.CrossRefGoogle Scholar
Lakowicz, J. R., Gryczynski, I., et al. (2000). Microsecond dynamics of biological macromolecules. Meth. Enzymol., 323, 473–509.CrossRefGoogle ScholarPubMed
Sportsman, J. R. (2003). Fluorescence anisotropy in pharmacologic screening. Meth. Enzymol., 361, 505–529.CrossRefGoogle ScholarPubMed
Lakowicz, J. R., Gryczynski, I., et al. (2000). Microsecond dynamics of biological macromolecules. Meth. Enzymol., 323, 473–509.CrossRefGoogle ScholarPubMed
Kroes, S. J., Canters, G. W., Giardi, G., Hoek, A., and Visser, A. J. W. G. (1998). Time-resolved fluorescence study of azurin variants: conformational heterogeneity and tryptophan mobility. Biophys. J., 75, 2441–2450.CrossRefGoogle ScholarPubMed
Lakovicz, J. R. (ed.). (1999) Principles of Fluorescence Spectroscopy, second edition. New York: Kluwer Academic/Plenum Publ.CrossRefGoogle Scholar
Cherry, R. J., and Schneider, G. (1976). A spectroscopic technique for measuring slow rotational diffusion of macromolecules. 2: Determination of rotational correlation times of protein in solution. Biochemistry, 15, 3657–3661.CrossRefGoogle Scholar
Ferrer, M. L., Duchowicz, R., Carrasco, B., Garcia de la Torre, J., and Acuna, A. U. (2001). The conformation of serum albumin in solution: a combined phosphorescence depolarization-hydrodynamic modeling study. Biophysical J., 80, 2422–2430.CrossRefGoogle ScholarPubMed
Millar, D. P. (2000). Time-resolved fluorescence methods for analysis of DNA–protein interactions. Meth. Enzymol., 323, 442–459.CrossRefGoogle ScholarPubMed
Hazlett, T. L., Moore, K. J. M., Lowe, P. N., Jameson, D. M., and Eccleston, J. F. (1993). Solution of p21ras proteins bound with fluorescent nucleotides: a time-resolved fluorescence study. Biochemistry, 32, 13575–13583.CrossRefGoogle ScholarPubMed
Canet, D., Doering, K., Dobson, C. M., and Dupont, Y. (2001). High-sensitivity fluorescence anisotropy detection of protein-folding events: Application to α−lactalbumin. Biophys. J., 80, 1996–2003.CrossRefGoogle ScholarPubMed

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