Pure and Applied Chemistry

Pure Appl. Chem., 2013, Vol. 85, No. 3, pp. 589-608

http://dx.doi.org/10.1351/PAC-REP-11-11-12

Published online 2013-01-11

ANALYTICAL CHEMISTRY DIVISION

ORGANIC AND BIOMOLECULAR CHEMISTRY DIVISION

PHYSICAL AND BIOPHYSICAL CHEMISTRY DIVISION

Fluorescence anisotropy measurements in solution: Methods and reference materials (IUPAC Technical Report)

References

• 1. J. Michl, E. W. Thulstrup. Spectroscopy with Polarized Light, VCH, New York (1986).
• 2. D. S. Kligger, J. W. Lewis, C. E. Randall. Polarized Light in Optics and Spectroscopy, Academic Press, New York (1990).
• 3a. B. Valeur. Molecular Fluorescence. Principles and Applications, Wiley-VCH, Weinheim (2002).
• 3b. B. Valeur, M. N. Berberan-Santos. Molecular Fluorescence. Principles and Applications, 2^nd ed., Wiley-VCH, Weinheim (2012).
• 4. J. R. Lakowicz. Principles of Fluorescence Spectroscopy, 3^rd ed., Springer, New York (2006).
• 5. C. A. Parker. Photoluminescence of Solutions, Elsevier, London (1968).
• 6a. R. F. Chen. Anal. Lett. 4, 459 (1971). (http://dx.doi.org/10.1080/00032717108058637)
• 6b. R. F. Chen. J. Res. Natl. Bur. Stand. A 76, 593 (1972). (http://dx.doi.org/10.6028/jres.076A.052)
• 7. K. Wojtuszewski, J. Knutson. In Protein Interactions: Biophysical Approaches for the Study of Complex Reversible Systems, P. Schuck (Ed.), pp. 397–416, Springer, New York (2007).
• 8. D. M. Jameson, G. Weber, R. D. Spencer, G. Mitchell. Rev. Sci. Instrum. 49, 510 (1978). (http://dx.doi.org/10.1063/1.1135451)
• 9. I. Gryczynski, H. Malak, J. R. Lakowicz. Chem. Phys. Lett. 245, 30 (1995). (http://dx.doi.org/10.1016/0009-2614(95)00958-7)
• 10. D. M. Jameson, J. C. Croney, P. D. J. Moens. In Methods in Enzymology, Vol. 360, G. Marriott, I. Parker (Eds.), pp. 1–43, Elsevier (2003).
• 11. R. E. Dale. In Time-Resolved Fluorescence Spectroscopy in Biochemistry and Biology, R. B. Cundall, R. E. Dale (Eds.), NATO ASI Series A: Life Sciences, Vol. 69, pp. 555–612, Plenum, New York (1983).
• 12. J. C. Owicki. J. Biomol. Screening 5, 297 (2000). (http://dx.doi.org/10.1177/108705710000500501)
• 13. T. Lindmo, H. B. Steen. Biophys. J. 18, 173 (1977). (http://dx.doi.org/10.1016/S0006-3495(77)85606-3)
• 14. C. A. Royer. Trends High Pressure Biosci. Biotechnol. 1–2, 17 (2002). (http://dx.doi.org/10.1016/S0921-0423(02)80074-0)
• 15. J. L. Markley, D. B. Northrup, C. A. Royer (Eds.). High Pressure Effects in Molecular Biophysics and Enzymology, Oxford University Press, Oxford (1996).
• 16. M. E. Jolley. J. Anal. Toxicol. 5, 236 (1986).
• 17. S. Y. Tetin. Anal. Biochem. 307, 84 (2002). (http://dx.doi.org/10.1016/S0003-2697(02)00011-8)
• 18. S. Y. Tetin, K. M. Swift, E. D. Matayoshi. Anal. Biochem. 307, 84 (2002). (http://dx.doi.org/10.1016/S0003-2697(02)00011-8)
• 19. S. Y. Tetin, T. L. Hazlett. Methods 20, 341 (2005). (http://dx.doi.org/10.1006/meth.1999.0927)
• 20. S. E. Braslavsky. Pure Appl. Chem. 79, 293 (2007). (http://dx.doi.org/10.1351/pac200779030293)
• 21. T. Azumi, S. P. McGlynn. J. Chem. Phys. 37, 2413 (1962). (http://dx.doi.org/10.1063/1.1733019)
• 22. Ch. Buehler, C. Y. Dong, P. T. C. So, T. French, E. Gratton. Biophys. J. 79, 536 (2000). (http://dx.doi.org/10.1016/S0006-3495(00)76315-6)
• 23. F. W. J. Teale. Photochem. Photobiol. 10, 363 (1969). (http://dx.doi.org/10.1111/j.1751-1097.1969.tb05701.x)
• 24. J. Eisinger, J. Flores. Biophys. J. 48, 77 (1985). (http://dx.doi.org/10.1016/S0006-3495(85)83761-9)
• 25. D. Jameson, J. C. Croney. Comb. Chem. High Throughput Screening 6, 167 (2003). (http://dx.doi.org/10.2174/138620703106298347)
• 26. H. P. Tschanz, T. H. Binkert. J. Phys. E: Sci. Instrum. 9, 1131 (1976). (http://dx.doi.org/10.1088/0022-3735/9/12/032)
• 27. S. R. Anderson, G. Weber. Biochemistry 8, 371 (1969). (http://dx.doi.org/10.1021/bi00829a051)
• 28. A. A. Paladini, G. Weber. Rev. Sci. Instrum. 52, 419 (1981). (http://dx.doi.org/10.1063/1.1136596)
• 29. A. A. Paladini, G. Weber. Biochemistry 20, 2587 (1981). (http://dx.doi.org/10.1021/bi00512a034)
• 30. P. Targowski, L. Davenport. Anal. Biochem. 274, 249 (1998). (http://dx.doi.org/10.1006/abio.1999.4252)
• 31. J. G. Zhou, S. Koulas, P. L.-G. Chong. Rev. Sci. Instrum. 71, 4249 (2000). (http://dx.doi.org/10.1063/1.1290036)
• 32. D. Axelrod. Biophys. J. 26, 557 (1979). (http://dx.doi.org/10.1016/S0006-3495(79)85271-6)
• 33. Q. Ruan, K. Ruan, C. Balny, M. Glaser, W. W. Mantulin. Biochemistry 40, 14706 (2001). (http://dx.doi.org/10.1021/bi010308i)
• 34. M. vandeVen, M. Ameloot, B. Valeur, N. Boens. J. Fluoresc. 15, 377 (2005). (http://dx.doi.org/10.1007/s10895-005-2632-1)
• 35. Commercially available from, e.g., Sigma-Aldrich, St. Louis, MO, USA.
• 36. O. Sire, B. Alpert, C. Royer. Biophys. J. 70, 2903 (1996). (http://dx.doi.org/10.1016/S0006-3495(96)79860-0)
• 37. R. B. Thompson, I. Gryczynski, J. Malicka. BioTechniques 32, 34 (2002).
• 38. L. B.-A. Johansson. J. Chem. Soc., Faraday Trans. 86, 2103 (1990). (http://dx.doi.org/10.1039/ft9908602103)
• 39. T. J. V. Prazeres, A. Fedorov, S. P. Barbosa, J. M. G. Martinho, M. N. Berberan-Santos. J. Phys. Chem. A 112, 5034 (2008). (http://dx.doi.org/10.1021/jp710625j)
• 40. G. Weber, F. J. Farris. Biochemistry 18, 3075 (1979). (http://dx.doi.org/10.1021/bi00581a025)
• 41. R. F. Chen, R. L. Bowman. Science 147, 729 (1965). (http://dx.doi.org/10.1126/science.147.3659.729)
• 42. J. R. Lakowicz, I. Gryczynski, Z. Gryczynski, J. D. Dattelbaum. Anal. Biochem. 267, 397 (1999). (http://dx.doi.org/10.1006/abio.1998.3029)
• 43. J. M. Beechem, E. Gratton, M. Ameloot, J. R. Knutson, L. Brand. In Topics in Fluorescence Spectroscopy, Vol. 2, J. R. Lakowicz (Ed.), pp. 241–305, Plenum, New York (1991).
• 44. J. P. Szubiakowski, R. E. Dale, N. Boens, M. Ameloot. J. Chem. Phys. 121, 7829 (2004). (http://dx.doi.org/10.1063/1.1798972)
• 45. A. Szabo. J. Chem. Phys. 81, 150 (1984). (http://dx.doi.org/10.1063/1.447378)
• 46. W. van der Meer, H. Pottel, W. Herreman, M. Ameloot, H. Hendrickx, H. Schröder. Biophys. J. 46, 515 (1984). (http://dx.doi.org/10.1016/S0006-3495(84)84049-7)
• 47. A. Arcioni, R. Tarroni, C. Zannoni. J. Chem. Soc., Faraday Trans. 89, 2815 (1993). (http://dx.doi.org/10.1039/ft9938902815)
• 48. W. E. Blumberg, R. E. Dale, J. Eisinger, D. Zuckerman. Biopolymers 13, 1589 (1974). (http://dx.doi.org/10.1002/bip.1974.360130808)
• 49. L. Brand, M. L. Johnson (Eds.). Numerical Computer Methods, Methods in Enzymology, Vol. 210, Academic, San Diego (1992).
• 50. Ph. Wahl. Biophys. Chem. 10, 91 (1979). (http://dx.doi.org/10.1016/0301-4622(79)80009-5)
• 51. C. W. Gilbert. In Time-Resolved Fuorescence Spectroscopy in Biochemistry and Biology, B. Cundall, R. E. Dale (Eds.), NATO ASI Series A: Life Sciences, Vol. 69, pp. 605–606, Plenum, New York (1983).
• 52. J. R. Knutson, J. M. Beechem, L. Brand. Chem. Phys. Lett. 102, 501 (1983). (http://dx.doi.org/10.1016/0009-2614(83)87454-5)
• 53. M. Ameloot, H. Hendrickx. Biophys. J. 44, 27 (1983). (http://dx.doi.org/10.1016/S0006-3495(83)84274-X)
• 54. A. Cross, G. R. Fleming. Biophys. J. 46, 45 (1984). (http://dx.doi.org/10.1016/S0006-3495(84)83997-1)
• 55. S. R. Flom, J. H. Fendler. J. Phys. Chem. 92, 5908 (1988). (http://dx.doi.org/10.1021/j100332a013)
• 56. M. Crutzen, M. Ameloot, N. Boens, R. M. Negri, F. C. De Schryver. J. Phys. Chem. 97, 8133 (1993). (http://dx.doi.org/10.1021/j100133a005)
• 57. N. Boens, W. Qin, N. Basari?, J. Hofkens, M. Ameloot, J. Pouget, J. P. Lefèvre, B. Valeur, E. Gratton, M. vandeVen, N. D. Silva, Y. Engelborghs, K. Willaert, A. Sillen, G. Rumbles, D. Phillips, A. J. W. G. Visser, A. van Hoek, J. R. Lakowicz, H. Malak, I. Gryczynski, A. G. Szabo, D. T. Krajcarski, N. Tamai, A. Miura. Anal. Chem. 79, 2137 (2007). (http://dx.doi.org/10.1021/ac062160k)
• 58. E. Feinstein, G. Deikus, E. Rusinova, E. L. Rachofsky, J. B. A. Ross, W. R. Laws. Biophys. J. 84, 599 (2003). (http://dx.doi.org/10.1016/S0006-3495(03)74880-2)
• 59. M. N. Berberan-Santos. J. Lumin. 50, 83 (1991). (http://dx.doi.org/10.1016/0022-2313(91)90022-N)
• 60. M. N. Berberan-Santos, P. Choppinet, A. Fedorov, L. Jullien, B. Valeur. J. Am. Chem. Soc. 122, 11876 (2000). (http://dx.doi.org/10.1021/ja000995l)
• 61. A. K. Livesey, J. C. Brochon. Biophys. J. 52, 693 (1987). (http://dx.doi.org/10.1016/S0006-3495(87)83264-2)
• 62. C. R. Mateo, P. Tauc, J. C. Brochon. Biophys. J. 65, 2248 (1993). (http://dx.doi.org/10.1016/S0006-3495(93)81258-X)
• 63. E. Gratton, D. M. Jameson, R. D. Hall. Ann. Rev. Biophys. Bioeng. 13, 105 (1984). (http://dx.doi.org/10.1146/annurev.bb.13.060184.000541)
• 64. G. B. Dutt, S. Doraiswamy, N. Periasamy, B. Venkataraman. J. Chem. Phys. 93, 8498 (1990). (http://dx.doi.org/10.1063/1.459288)
• 65. J. Beechem, M. Ameloot, L. Brand. Anal. Instrum. 14, 379 (1985). (http://dx.doi.org/10.1080/10739148508543585)
• 66. M. D. Barkley, A. A. Kowalczyk, L. Brand. J. Chem. Phys. 75, 3581 (1981). (http://dx.doi.org/10.1063/1.442468)
• 67. A. Balter, J. Szubiakowski. J. Fluoresc. 3, 247 (1993). (http://dx.doi.org/10.1007/BF00865272)
• 68. J. Szubiakowski, A. Balter, W. Novak, A. Kowalczyk, K. Wisniewski, M. Wierzbowska. Chem. Phys. 208, 283 (1996). (http://dx.doi.org/10.1016/0301-0104(96)00104-8)
• 69. N. Boens, M. Ameloot. Int. J. Quantum Chem. 106, 300 (2006). (http://dx.doi.org/10.1002/qua.20752)
• 70. N. Boens, E. Novikov, M. Ameloot. ChemPhysChem 7, 2559 (2006). (http://dx.doi.org/10.1002/cphc.200600309)
• 71. N. Boens, E. Novikov, J. P. Szubiakowski, M. Ameloot. J. Phys. Chem. A 109, 11655 (2005). (http://dx.doi.org/10.1021/jp054797y)
• 72. J. P. Szubiakowski, R. E. Dale, N. Boens, M. Ameloot. Chem. Phys. Lett. 438, 113 (2007). (http://dx.doi.org/10.1016/j.cplett.2007.02.051)
• 73. G. J. Blanchard, C. A. Cibal. J. Phys. Chem. 92, 5950 (1988). (http://dx.doi.org/10.1021/j100332a022)
• 74. G. S. Beddard, T. Doust, G. Porter. Chem. Phys. 61, 17 (1981). (http://dx.doi.org/10.1016/0301-0104(81)85044-6)
• 75. A. Volkmer, D. Hatrick, D. J. S. Birch. Meas. Sci. Technol. 8, 1339 (1997). (http://dx.doi.org/10.1088/0957-0233/8/11/021)
• 76. A. Volkmer, V. Subramaniam, D. J. S. Birch, T. M. Jovin. Biophys. J. 78, 1589 (2000). (http://dx.doi.org/10.1016/S0006-3495(00)76711-7)