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Chapter F3 - Fluorescence microscopy

from Part F - Optical microscopy

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

Historical review

1931

M. Goppert-Mayer gave the theoretical background of two-photon excitation in fluorescence. Thirty years later this phenomenon was observed experimentally shortly after the invention of the laser by W. Kaiser and C. Garrett. In 1990 W. Denk introduced two-photon excitation in fluorescent microscopy.

1948

T. Forster formulated the principle of fluorescence resonance energy transfer (FRET), a phenomenon that occurs when two different chromophores (donor and acceptor) with overlapping emission/absorption spectra are separated by a suitable orientation and a distance in the range 20–100 Å. In the early 1970s, after a long period of inaction, the ground-breaking work of L. Stryer and R. P Hohland on FRET revealed the spatial proximity relationships of two fluorescence-labelled sites in biological macromolecules, thereby establishing FRET as a spectroscopic ruler. All of this early work used either fluorescent analogues of biomolecules or fluorescent reagents covalently or non-covalently attached to macromolecules as donors or acceptors of FRET. In the 1990s the introduction of the green fluorescent protein (GFP) to FRET-based imaging microscopy gave new life to its use as a sensitive probe of protein–protein interactions and protein conformational changes in vivo.

1964

S. Singh and L. Bradely predicted a three-photon absorption mechanism. In 1995 three-photon excited fluorescence spectroscopy and microscopy was demonstrated by a few groups and applied to the imaging of biological specimens and live cells.

Early 1970s

The first lifetime measurements on single points under a microscope were carried out by a few groups.

Type
Chapter
Information
Methods in Molecular Biophysics
Structure, Dynamics, Function
 , pp. 658 - 682
Publisher: Cambridge University Press
Print publication year: 2007

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References

Lakovicz, J. R. (ed.) (1999). Principles of Fluorescence Spectroscopy, second edition. New York: Academic / Plenum Publ.CrossRefGoogle Scholar
Herman, B., and Jacobson, K., (eds.) (1990). Optical Microscopy for Biology. New York: Wiley-Liss.Google Scholar
Tamm, L. K. (1993). Total internal reflectance fluorescence microscopy. In Optical Microscopy. Emerging Methods and Applications. Eds Herman, B. and Lemasters, J. J., Academic Press.Google Scholar
Piston, D. W. (1999). Imaging living cells and tissues by two-photon excitation microscopy. Trends Cell Biol., 9, 66–69.CrossRefGoogle ScholarPubMed
Gustafsson, M. G. L. (1999). Extended resolution fluorescence microscopy. Curr. Opin. Struct. Biol., 9, 627–634.CrossRefGoogle ScholarPubMed
Weiss, S. (2000). Shattering the diffraction limit of light: a revolution in fluorescence microscopy? Proc. Nat. Acad. Sci. USA., 97, 8747–8749.CrossRefGoogle ScholarPubMed
Schrader, M., Bahlmann, K., Giese, G., and Hell, S. W. (1998). 4Pi-confocal imaging in fixed biological specimens. Biophys. J., 75, 1659–1668.CrossRefGoogle ScholarPubMed
Nagorni, M., and Hell, S. W. (1998). 4Pi-Confocal microscopy provides three-dimensional images of the microtubule network with 100-to-150 nm resolution. J. Struct. Biol., 123, 236–247.CrossRefGoogle ScholarPubMed
Cragg, G. E., and So, P. T. C. (2000). Lateral resolution enhancement with standing evanescent waves. Opt. Lett., 25, 46–48.CrossRefGoogle ScholarPubMed
Klar, T. A., Jacobs, S., Dyba, M., Egner, A., and Hell, S. W. (2000). Fluorescence microscopy with diffraction resolution barrier broken by stimulated emission. Proc. Natl. Acad. Sci. USA, 97, 8206–8210.CrossRefGoogle ScholarPubMed
Stryer, L. (1978). Fluorescence energy transfer as a spectroscopic ruler. Annu. Rev. Biochem., 47, 819–846.CrossRefGoogle ScholarPubMed
Selvin, P. R. (2000). The renaissance of fluorescence resonance energy transfer. Nature Str. Biol., 7, 730–734.CrossRefGoogle ScholarPubMed
Hillisch, A., Lorenz, M., and Diekmann, S. (2001). Recent advances in FRET: distance determination in protein-DNA complexes. Curr. Opin. Struct. Biol., 11, 201–207.CrossRefGoogle ScholarPubMed
Tcien, R. Y. (1998). The green fluorescent protein. Annu. Rev. Biochem., 67, 509–544.Google Scholar
Ellenberg, J., Lippincot-Schwartz, J., and Presly, J. F. (1999). Dual-colour imaging with GFP variants. Trends Cell Biol., 9, 52–60.CrossRefGoogle ScholarPubMed
Bastiaens, P. I. H., and Squire, A. (1999). Fluorescence lifetime imaging microscopy: spatial resolution of biochemical processes in the cell. Trends Cell Biol., 9, 48–52.CrossRefGoogle Scholar
Tcien, R. Y., and Miyawaki, A. (1998). Seeing the machinery of live cells. Science, 280, 1954–1955.Google Scholar
Piston, D. W. (1999). Imaging living cells and tissues by two-photon excitation microscopy. Trends Cell Biol., 9, 66–69.CrossRefGoogle ScholarPubMed
Bastiaens, P. I. H., and Pepperkok, R. (2000). Observing proteins in their natural habitat: the living cell. TIBS, 25, 631–636.Google ScholarPubMed
Lakovicz, J. R. (ed.) (1999). Principles of Fluorescence Spectroscopy, second edition. New York: Academic / Plenum Publ.CrossRefGoogle Scholar
Herman, B., and Jacobson, K., (eds.) (1990). Optical Microscopy for Biology. New York: Wiley-Liss.Google Scholar
Tamm, L. K. (1993). Total internal reflectance fluorescence microscopy. In Optical Microscopy. Emerging Methods and Applications. Eds Herman, B. and Lemasters, J. J., Academic Press.Google Scholar
Piston, D. W. (1999). Imaging living cells and tissues by two-photon excitation microscopy. Trends Cell Biol., 9, 66–69.CrossRefGoogle ScholarPubMed
Gustafsson, M. G. L. (1999). Extended resolution fluorescence microscopy. Curr. Opin. Struct. Biol., 9, 627–634.CrossRefGoogle ScholarPubMed
Weiss, S. (2000). Shattering the diffraction limit of light: a revolution in fluorescence microscopy? Proc. Nat. Acad. Sci. USA., 97, 8747–8749.CrossRefGoogle ScholarPubMed
Schrader, M., Bahlmann, K., Giese, G., and Hell, S. W. (1998). 4Pi-confocal imaging in fixed biological specimens. Biophys. J., 75, 1659–1668.CrossRefGoogle ScholarPubMed
Nagorni, M., and Hell, S. W. (1998). 4Pi-Confocal microscopy provides three-dimensional images of the microtubule network with 100-to-150 nm resolution. J. Struct. Biol., 123, 236–247.CrossRefGoogle ScholarPubMed
Cragg, G. E., and So, P. T. C. (2000). Lateral resolution enhancement with standing evanescent waves. Opt. Lett., 25, 46–48.CrossRefGoogle ScholarPubMed
Klar, T. A., Jacobs, S., Dyba, M., Egner, A., and Hell, S. W. (2000). Fluorescence microscopy with diffraction resolution barrier broken by stimulated emission. Proc. Natl. Acad. Sci. USA, 97, 8206–8210.CrossRefGoogle ScholarPubMed
Stryer, L. (1978). Fluorescence energy transfer as a spectroscopic ruler. Annu. Rev. Biochem., 47, 819–846.CrossRefGoogle ScholarPubMed
Selvin, P. R. (2000). The renaissance of fluorescence resonance energy transfer. Nature Str. Biol., 7, 730–734.CrossRefGoogle ScholarPubMed
Hillisch, A., Lorenz, M., and Diekmann, S. (2001). Recent advances in FRET: distance determination in protein-DNA complexes. Curr. Opin. Struct. Biol., 11, 201–207.CrossRefGoogle ScholarPubMed
Tcien, R. Y. (1998). The green fluorescent protein. Annu. Rev. Biochem., 67, 509–544.Google Scholar
Ellenberg, J., Lippincot-Schwartz, J., and Presly, J. F. (1999). Dual-colour imaging with GFP variants. Trends Cell Biol., 9, 52–60.CrossRefGoogle ScholarPubMed
Bastiaens, P. I. H., and Squire, A. (1999). Fluorescence lifetime imaging microscopy: spatial resolution of biochemical processes in the cell. Trends Cell Biol., 9, 48–52.CrossRefGoogle Scholar
Tcien, R. Y., and Miyawaki, A. (1998). Seeing the machinery of live cells. Science, 280, 1954–1955.Google Scholar
Piston, D. W. (1999). Imaging living cells and tissues by two-photon excitation microscopy. Trends Cell Biol., 9, 66–69.CrossRefGoogle ScholarPubMed
Bastiaens, P. I. H., and Pepperkok, R. (2000). Observing proteins in their natural habitat: the living cell. TIBS, 25, 631–636.Google ScholarPubMed

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