Fluorescence resonance energy transfer in studies of inter-chromophoric distances in biomolecules

Acta Biochimica Polonica

Volumn 44, Issue 3, 1997, Pages 477-490

  Łankiewicz, Leszek ^a   Malicka, Joanna ^a   Wiczk, Wiesław ^a  

^a UNIVERSITY OF GDA SK   (Poland)

Author keywords

Biomolecule; Conformation; Fluorescence resonance energy transfer; Interchromophoric distance; Proteins

Indexed keywords

PROTEIN CONFORMATION; REVIEW; SPECTROFLUOROMETRY;

PROTEIN CONFORMATION; SPECTROMETRY, FLUORESCENCE;

EID: 0031299174     PISSN: 0001527X     EISSN: None     Source Type: Journal    
DOI: 10.18388/abp.1997_4398     Document Type: Review

References (95)

1. Förster, T. (1948) Intramolecular energy migration and fluorescence. Ann. Phys. (Leipzig) 2, 55-75, English translation by Knox, R.S., University of Rochester, 1974.
2. Förster, T. (1948) Intramolecular energy migration and fluorescence. Ann. Phys. (Leipzig) 2, 55-75, English translation by Knox, R.S., University of Rochester, 1974.
3. Förster, T. (1959) Transfer mechanism of electronic excitation. Discus. Faraday Soc. 27, 7-17.
4. Förster, T. (1960) Transfer mechanism of electronic excitation energy. Radiat. Res. Suppl. 2, 326-339.
5. Förster, T. (1965) Delocalized excitation and excitation transfer; in Modern Quantum Chemistry (Sinanoglu, O., ed.) vol. 3, pp. 93-137, Academic Press, New York.
6. Turro, N.J. (1977) Energy transfer processes. Pure Appl. Chem. 49, 405-429.
7. Speiser, S. (1996) Photophysics and mechanism of intramolecular electronic energy transfer in bichromophoric system: Solution and supersonic jet studies. Chem. Rev. 96, 1953-1976.
8. Clegg, R.M. (1996) Fluorescence resonance energy transfer; in Fluorescence Imaging Spectroscopy and Microscopy (Wang, X.F. & Herman, B., eds.) Chemical Analysis Series, vol. 137, John Wiley & Sons Inc., New York.
9. Dexter, D.L. (1953) A theory of sensitized luminescence in solids. J. Chem. Phys. 21, 836-850.
10. Jovin, T.M. & Jovin-Arndt, D. (1989) Luminescence digital imaging microscopy. Annu. Rev. Biophys. Chem. 18, 271-308.
11. Young, R.M., Arnette, J.K., Roess, D.A. & Barisas, B.G. (1994) Quantitation of fluorescence energy transfer between cell surface proteins via fluorescence donor photobleaching kinetics. Biophys. J. 67, 881-888.
12. Mekler, M.V. (1994) A photochemical technique to enhance sensitivity of detection of fluorescence resonance energy transfer. Photochem. Photobiol. 59, 615-620.
13. Schiller, P. (1985) Application of fluorescence techniques in studies of peptide conformation and interaction. Peptides 7, 116-164.
14. Fairclough, R.H. & Cantor, C.R. (1978) The use of singlet-singlet energy transfer to study macromolecular assemblies. Methods Enzymol. 48, 347-379.
15. Mugnier, J., Pouget, J., Bourson, J. & Valeur, B. (1985) Efficiency of intramolecular electronic energy transfer in coumarin bichromophoric molecules. J. Luminescence 33, 273-300.
16. Clegg, R.M. (1992) Fluorescence resonance energy transfer and nucleic acid. Methods Enzymol. 211, 353-388.
17. Wu, P. & Brand, L. (1994) Resonance energy transfer: Methods and application. Anal. Biochem. 218, 1-13.
18. Selvin, P.R. (1995) Fluorescence resonance energy transfer. Methods Enzymol. 246, 300-334.
19. Wiczk, W. & Łankiewicz, L. (1996) Average distance and distance distribution estimation by steady-state energy transfer measurement. Wiad. Chemiczne 50, 99-124, (in Polish).
20. Wiczk, W. (1996) Application of Radiationless Energy Transfer in Studies of Conformation of Biologically Active Compounds. Habilitation dissertation, Wyd. Uniwersytetu Gdańskiego, Gdańsk, (in Polish).
21. Cheung, H.C. (1991) Resonance energy transfer; in Topics in Fluorescence Spectroscopy (Lakowicz, J.R., ed.) vol. 2, Principles, pp. 127-171, Plenum Press, New York.
22. Schiller, P. (1975) Intramolecular distances: Energy transfer; in Biochemical Fluorescence: Concepts (Chen, R.F. & Edelhoch, H., eds.) vol. 1, pp. 258-303, Marcel Dekker, New York.
23. Stryer, L. & Haugland, R.P. (1967) Energy transfer: A spectroscopic ruler. Proc. Natl. Acad. Sci. U.S.A. 58, 719-726.
24. Stryer, L. (1978) Fluorescence energy transfer as a spectroscopic ruler. Annu. Rev. Biochem. 47, 819-846.
25. Steinberg, I.Z. (1971) Long-range nonradiative transfer of electronic energy in protein and peptides. Annu. Rev. Biochem. 40, 83-114.
26. Mathis, G. (1993) Rare earth cryptants and homogeneous fluoroimmunoassays with human sera. Clin. Chem. 39, 1953-1959.
27. Dos Remedios, C.G. & Moens, P.D. (1995) Fluorescence resonance energy transfer spectroscopy is a reliable "ruler" for measuring structural changes in proteins. J. Struc. Biol. 115, 175-185.
28. Dos Remedios, C.G., Miki, M. & Barden, J.A. (1987) Fluorescence resonance energy transfer measurements of distance in actin and myosin: A critical evaluation. J. Muscle Res. Cell Motil. 8, 97-118.
29. Amir, D. & Haas, E. (1987) Estimation of intramolecular distance distribution in bovine pancreatic trypsin inhibitor by site-specific labeling and nonradiative excitation energy-transfer measurements. Biochemistry 26, 2162-2175.
30. Haas, E. (1986) Folding and dynamics of proteins studied by non-radiative energy transfer measurements; in Photophysical and Photochemical Tools in Polymer Science (Winnik, M.A., ed.) pp. 325-350, D. Reidel Publishing Comp., Dordrecht.
31. Harton, H.R. & Koshland, D.E. (1967) Environmentally sensitive groups attached to proteins. Methods Enzymol. 11, 857-870.
32. Forster, Y. & Hass, E. (1993) Preparation and characterization of three fluorescent labels for proteins, suitable for structural studies. Anal. Biochem. 209, 9-14.
33. Corrie, J.E.T. (1994) Thiol-reactive fluorescent probes for protein labeling. J. Chem. Soc. Perkin Trans. I, 2975-2982.
34. Waggogner, A. (1995) Covalent labeling of protein and nucleic acid with fluorofores. Methods Enzymol. 246, 363-373.
35. Haugland, R.P. (1996) Handbook of Fluorescent Probes and Research Chemical. Molecular Probes, 6th edn.
36. Cantor, C.R. & Pechukas, P. (1971) Determination of distance distribution functions by singlet-singlet energy transfer. Proc. Natl. Acad. Sci. U.S.A. 68, 2099-2101.
37. Gryczynski, I., Wiczk, W., Johnson, M.L., Cheung, H.C., Wang, C. & Lakowicz, J.R. (1988) Resolution of the end-to-end distance distribution of flexible molecules using quenching-induced variations Förster distance for fluorescence energy transfer. Biophys. J. 54, 577-586.
38. Wiczk, W., Eis, P.S., Fishman, M.N., Johnson, M.L. & Lakowicz, J.R. (1991) Distance distributions recovered from steady-state fluorescence measurements on thirteen donor-acceptor pairs with different Förster distance. J. Fluorescence 1, 273-286.
39. Gryczynski, I., Wiczk, W., Johnson, M.L. & Lakowicz, J.R. (1988) End-to-end distance distributions of flexible molecules from steady state fluorescence energy transfer and quenching-induced changes in the Förster distance. Chem. Phys. Lett. 145, 439-446.
40. Wiczk, W., Gryczynski, I., Szmacinski, H., Johnson, M.L., Kruszynski, M. & Zboinska, J. (1988) Distribution of distances in thiopeptides by fluorescence energy transfer and frequency-domain fluorometry. Biophys. Chem. 32, 43-49.
41. Szmacinski, H., Wiczk, W., Fishman, M.N., Eis, P.S., Lakowicz, J.R. & Johnson, M.L. (1996) Distance distributions from the tyrosyl to disulfide residues in oxytocin and [Arg8]-vasopressin measured using frequency-domain fluorescence resonance energy transfer. Eur. Biophys. J. 24, 185-194.
42. Eis, P.S. & Lakowicz, J.R. (1993) Time-resolved energy transfer measurements of donor-acceptor distance distribution and intramolecular flexibility of CCHH zinc finger peptide. Biochemistry 32, 7981-7993.
43. Lakowicz, J.R., Gryczynski, I., Wiczk, W., Laczko, G., Prendergast, F.C. & Johnson, M.L. (1990) Conformational distributions of melittin in water-methanol mixtures from frequency-domain measurements of non-radiative energy transfer. Biophys. Chem. 36, 99-115.
44. Beals, J.M., Haas, E., Krausz, S. & Scheraga, H.A. (1991) Conformational studies of a peptide corresponding to a region of the C-terminus of ribonuclease A: Implication as a potential chain-folding initiation site. Biochemistry 30, 7680-7692.
45. Haas, E., Wilchek, M., Katchalski-Katzir, E. & Steinberg, I.Z. (1975) Distribution of end-to-end distances of oligopeptides in solution as estimated by energy transfer. Proc. Natl. Acad. Sci. U.S.A. 72, 1807-1811.
46. Cheung, H.C., Gryczynski, I., Malak, H., Wiczk, W., Johnson, M.L. & Lakowicz, J.R. (1991) Conformational flexibility of the Cys 697-Cys 707 segment of myosin subfragment-1: Distance distribution by frequency-domain fluorometry. Biophys. Chem. 40, 1-17.
47. Amir, D. & Haas, E. (1986) Determination of intramolecular distance distribution in a globular protein by nonradiative excitation energy transfer measurements. Biopolymers 25, 235-240.
48. Gottfried, D.S. & Haas, E. (1992) Nonlocal interaction stabilize folding intermediates in reduced unfolded bovine pancreatic trypsin inhibitor. Biochemistry 31, 12353-12362.
49. Lakowicz, J.R., Gryczynski, I., Cheung, H.C. & Wang, C. (1988) Distance distribution in native and random-coiled troponin I from frequency-domain measurements of fluorescence energy transfer. Biopolymers 27, 821-830.
50. Cheung, H.C., Wang, C., Gryczynski, I., Wiczk, W., Laczko, G., Johnson, M.L. & Lakowicz, J.R. (1991) Distance distributions and anisotropy decays of troponin C and its complex with troponin I. Biochemistry 30, 5238-5247.
51. Wu, P.G., James, E. & Brand, L. (1993) Compact thermally-denaturated state of a staphylococcal nuclease mutant from resonance energy transfer measurements. Biophys. Chem. 46, 123-133.
52. James, E., Wu, P.G., Stites, W. & Brand, L. (1992) Compact denaturated state of a staphylococcal nuclease mutant by guanidinium as determined by resonance energy transfer. Biochemistry 31, 10217-10225.
53. McWherter, C.A., Haas, E., Leed, A.R. & Scheraga, H.A. (1986) Conformational unfolding in the N-terminal region of ribonuclease A detected by nonradiative energy transfer. Biochemistry 25, 1951-1963.
54. Haas, E., McWherter, C.A. & Scheraga, H.A. (1988) Conformational unfolding in the N-terminal region of ribonuclease A detected by nonradiative energy transfer: Distribution of interresidue distance in the native, denaturated, and reduced-denaturated states. Biopolymers 27, 1-21.
55. Rice, K.G., Wu, P., Brand, L. & Lee, Y.C. (1991) Interterminal distance and flexibility of a triantennary glycopeptide as measured by resonance energy transfer. Biochemistry 30, 6646-6655.
56. Wu, P., Rice, K.G., Brand, L. & Lee, Y.C. (1991) Differential flexibility in three branches of an N-linked triantennary glycopeptide. Proc. Natl. Acad. Sci. U.S.A. 88, 9355-9359.
57. Maliwal, B.P., Kuśba, J., Wiczk, W., Johnson, M.L. & Lakowicz, J.R. (1993) End-to-end diffusion coefficients and distance distributions from fluorescence energy transfer measurements: Enhanced resolution by using multiple acceptors with different Förster distances. Biophys. Chem. 46, 273-281.
58. Lakowicz, J.R., Gryczyński, I., Kuśba, J., Wiczk, W., Szmaciński, H. & Johnson, M.L. (1994) Site-to-site diffusion in proteins as observed by energy transfer and frequency-domain fluorometry. Photochem. Photobiol. 59, 16-29.
59. Lakowicz, J.R., Kusba, J. & Wiczk, W. (1990) Influence of end-to-end diffusion on intramolecular energy transfer as observed by frequency-domain fluorometry. Biophys. Chem. 38, 99-109.
60. Dale, R.E. & Eisinger, J. (1974) Intramolecular distances determined by energy transfer. Dependence on orientational freedom of donor and acceptor. Biopolymers 13, 1573-1605.
61. Dale, R.E., Eisinger, J. & Blumberg, W.E. (1979) The orientational freedom of molecular probes. The orientation factor in intramolecular energy transfer. Biophys. J. 26, 161-194.
62. Censullo, R., Martin, J.C. & Cheung, H.C. (1992) The use of isotropic orientation factor in fluorescence energy transfer (FRET) studies of the actin filament. J. Fluorescence 2, 141-155.
63. Haas, E. & Katchalski-Katzir, E. (1978) Effect of the orientation of donor and acceptor on the probability of energy transfer involving electronic transition of mixed polarization. Biochemistry 17, 5064-5070.
64. Horrocks, W. De W., Jr. (1993) Luminescence spectroscopy. Methods Enzymol. 226, 495-538.
65. Lakowicz, J.R., Gryczynski, I., Wiczk, W., Laczko, G., Prendergast, F.G. & Johnson, M.L. (1990) Conformational distributions of melittin in water-methanol mixtures from frequency-domain measurements of non-radiative energy transfer. Biophys. Chem. 36, 99-115.
66. Guillard, R. & Englert, A. (1976) Interpretation of energy-transfer experiments by theoretical studies of model compounds using semiempirical potential functions. I. Three-linked aromatic peptide unit. Biopolymers 15, 1301-1314.
67. Leclerc, M., Premilat, S. & Englert, A. (1978) Nonradiative energy transfer in oligopeptide chain generated by a Monte Carlo method including long-range interactions. Biopolymers 17, 2459-2473.
68. Leclerc, M., Premilat, S., Guillard, R., Renneboog-Squilbin, C. & Englert, A. (1977) Interpretation of energy transfer experiments by theoretical studies of model compounds using semiempirical potential functions. II. Monte Carlo calculations on oligopeptides. Biopolymers 16, 531-544.
69. Steinberg, I.Z. (1968) Nonradiative energy transfer in systems in which rotatory Brownian motion is frozen. J. Chem. Phys. 48, 2411-2413.
70. Steinberg, I.Z, Haas, E. & Katchalski-Katzir, E. (1983) Long-range nonradiative transfer of electronic excitation energy; in Time-resolved Fluorescence Spectroscopy in Biochemistry and Biology (Cundall, R.B. & Dale, R.B., eds.) vol. 69, pp. 411-450, Plenum Press, New York.
71. Wu, P. & Brand, L. (1992) Orientation factor in steady-state and time-resolved resonance energy transfer measurements. Biochemistry 31, 7939-7947.
72. Eis, P.S. & Millar, D.P. (1993) Conformational distributions of a four-way DNA junction revealed by time-resolved fluorescence resonance energy transfer. Biochemistry 32, 13852-13860.
73. Lakowicz, J.R., Gryczynski, I., Wiczk, W., Kusba, J. & Johnson, M.L. (1991) Correction for incomplete labeling in distance distributions determined by frequency-domain fluorometry. Anal. Biochem. 195, 243-254.
74. Lakowicz, J.R., Kusba, J., Szmacinski, H., Gryczynski, I., Eis, P.S., Wiczk, W. & Johnson, M.L. (1991) Resolution of end-to-end diffusion coefficients and distance distributions of flexible molecules using fluorescent donor-acceptor and donor-quencher pairs. Biopolymers 31, 1363-1378.
75. Horrocks, W. De W., Jr., Holmquist, B. & Vallee, B.L. (1975) Energy transfer between terbium (III) and cobalt (II) in thermolysin: A new class of metal-metal distance probes. Proc. Natl. Acad. Sci. U.S.A. 72, 4764-4768.
76. Matthews, B.W., Weaver, L.H. & Kester, W.R. (1974) The conformation of thermolysin. J. Biol. Chem. 249, 8030-8044.
77. Horrocks, W. De W., Jr. & Tingey, J.M. (1988) Time-resolved europium (III) luminescence excitation spectroscopy: Characterization of calcium-binding sites of calmodulin. Biochemistry 27, 413-419.
78. Babu, Y.S., Bugg, C.E. & Cook, W.J. (1988) Structure of calmodulin refined at 2.2 Å resolution. J. Mol. Biol. 204, 191-204.
79. Snider, A.P., Sudnick, D.R., Arkle, V.K. & Horrocks, W. De W., Jr. (1981) Lanthanide ion luminescence probes. Characterization of metal ion binding sites and intermetal energy transfer distance measurements in calcium-binding proteins. 2. Thermolysin. Biochemistry 20, 3334-3339.
80. Rhee, M.-J., Sudnick, D.R., Arkle, V.K. & Horrocks, W. De W., Jr. (1981) Lanthanide ion luminescence probes. Characterization of metal ion binding sites and intermetal energy transfer distance measurements in calcium-binding proteins. 1. Parvalbumin. Biochemistry 20, 3328-3334.
81. Rhee, M.-J., Horrocks, W. De W., Jr. & Kosow, D.P. (1984) Laser-induced lanthanide luminescence as a probe of metal ion-binding sites of human Factor Xa. J. Biol. Chem. 259, 7404-7408.
82. McWherter, C.A., Haas, E., Leed, A.R. & Scheraga, H.A. (1986) Conformational unfolding in the N-terminal region of ribonuclease A detected by nonradiative energy transfer. Biochemistry 25, 1951-1963.
83. Borkakoti, N., Moss, D.S. & Palmer, R.A. (1982) Ribonuclease-A: Least-squares refinement of the structure at 1.45 Å resolution. Acta Crystallogr., Sec. B: Struct. Crystallogr. Cryst. Chem. 38B, 2210-2217.
84. Wlodawer, A., Walter, J., Huber, R. & Sjolin, L. (1984) Structure of bovine pancreatic trypsin inhibitor. Results of joint neutron and X-ray refinement of crystal form II. J. Mol. Biol. 180, 301-329.
85. Kabsch, W., Mannherz, H.G., Suck, D., Pai, E.F. & Holmes, K.C. (1990) Atomic structure of the actin-DNase I complex. Nature 347, 37-44.
86. Miki, M., O'Donoghue, S.I. & Dos Remedios, C.G. (1992) Structure of actin observed by fluorescence resonance energy transfer spectroscopy. J. Muscle Res. Cell Motil. 13, 132-145.
87. O'Donoghue, S.I., Hambly, B.D. & Dos Remedios, C.G. (1992) Models of actin monomer and filament from fluorescence resonance energy transfer. Eur. J. Biochem. 205, 591-601.
88. McLaughlin, P.J., Gooch, P.J., Mannherz, H.G. & Weeds, A.G. (1993) Structure of gelsolin segment-1-actin complex and the mechanism of filament severing. Nature 364, 685-692.
89. Schutt, C.E., Myslik, J.C., Rozycki, M.D., Goonesekere, N.C.W. & Lindberg, U. (1993) The structure of crystalline profilin-β-actin. Nature 365, 810-816.
90. Lorenz, M., Popp, D. & Holmes, K.C. (1993) Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 234, 826-836.
91. Dos Remedios, C.G. & Moens, P.D.J. (1995) Actin and the actinomyosin interface. Biochim. Biophys. Acta 1228, 99-124.
92. Lauterwein, J., Brown, L.R. & Würtrich, K. (1980) High-resolution 1H-NMR studies of monomeric melittin in aqueous solution. Biochim. Biophys. Acta 622, 219-230.
93. Bazzo, R., Tappin, M.J., Pastore, A., Harvey, T.S., Carver, J.A. & Campbell, D. (1988) The structure of melittin. A 1H-NMR study in methanol. Eur. J. Biochem. 173, 139-146.
94. Brown, L.R. & Wütrich, K. (1981) Melittin bounded to dodecylphosphatocholine micelles. 1H-NMR assigments and global conformational features. Biochim. Biophys. Acta 647, 95-111.
95. Lakowicz, J.R., Gryczynski, I., Laczko, G., Wiczk, W. & Johnson, M.L. (1994) Distribution of distances between tryptophan and the N-terminal residue of melittin in its complex with calmodulin, troponin C, and phospholipids. Protein Sci. 3, 628-637.