Biophysics of the green fluorescent protein

Methods in Cell Biology

Volumn , Issue 58, 1999, Pages 1-18

  Prendergast, F G ^a  

^a MAYO CLINIC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GREEN FLUORESCENT PROTEIN; GUANOSINE TRIPHOSPHATE; PHOTOPROTEIN;

ANIMAL; CHEMISTRY; PROTEIN CONFORMATION; PROTEIN FOLDING; REVIEW;

ANIMALS; GREEN FLUORESCENT PROTEINS; GUANOSINE TRIPHOSPHATE; LUMINESCENT PROTEINS; PROTEIN CONFORMATION; PROTEIN FOLDING;

EID: 0032621293     PISSN: 0091679X     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Article

References (39)

1. Blinks, J. R., Prendergast, F. G., and Allen, D. G. (1978). Photoproteins as biological calcium indicators. Pharmacol. Rev. 28, 1-93.
2. Branchini, B. R., Lusins, J. O., and Zimmer, M. (1997). A molecular mechanics and database analysis of the structural preorganization and activation of the chromophore-containing hexapeptide fragment in green fluorescent protein. J. Biomolecular Structure and Dynamics 14, 441-448.
3. Brejc, K., Sixma, T. K., Kitts, P. A., Kain, S. R., Tsien, R. Y., Ormö, M., and Remington, S. J. (1997). Structural basis for dual excitation and photoisomerization of the Aequorea victoria green fluorescent protein. Proc. Natl. Acad. Sci. U. S. A. 94, 2306-2311.
4. Chalfie, M., Tu, Y., Euskirchen, G., Ward, W. W., and Prasher, D. C. (1994). Green fluorescent protein as a marker for gene expression. Science 263, 802-804.
5. Chattoraj, M., King, B. A., Bublitz, G., and Boxer, S. G. (1996). Ultra-fast excited state dynamics in green fluorescent protein: multiple states and proton transfer. Proc. Natl. Acad. Sci. U. S. A. 93, 8362-8367.
6. Clark, P. L., Liu, Z. P., Rizo, J., and Gierasch, L. M. (1997). Cavity formation before stable hydrogen bonding in the folding of a β-clam protein. Nat. Struct. Biol. 4, 883-886.
7. Cody, C. W., Prasher, D. C., Westler, W. M., Prendergast, F. G., and Ward, W. W. (1993). Chemical structure of the hexapeptide chromophore of the Aequorea green fluorescent protein. Biochemistry 32, 1212-1218.
8. Delagrave, S., Hautin, R. E., Silva, C. M., Yang, M. M., and Youvan, D. C. (1995). Red-shifted excitation mutants of the green fluorescent protein. Biotechnology 13, 151-154.
9. Haydock, C. (1993). Protein side chain rotational isomerization: A minimum perturbation mapping study. J. Chem. Phys. 98, 8199-8214.
10. Heim, R., Prasher, D. C., and Tsien, R. Y. (1994). Wavelength mutations and post-translational autoxidation of green fluorescent protein. Proc. Natl. Acad. Sci. U. S. A. 91, 12501-12504.
11. Kauzmann, W. (1954). In "The Mechanism of Enzyme Action" (McElroy, W. D., and Glass, B., Eds.) pp. 70-120. Johns Hopkins Press, Baltimore, Maryland.
12. Kidwai, A. R., and Devasia, G. M. (1962). A new method for the synthesis of amino acids. Synthesis of amino acids and their derivatives through 2,4-disubstituted 2-imidazolin-5-ones. J. Org. Chem. 27, 4527-4531.
13. Kim, P. S., and Baldwin, R. L. (1990). Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59, 631-660.
14. Kjaer, A. (1953). Reactions between amino esters and α-amino acid esters Part III: 2-phenyl-5(4)Imidazolone and its reactions.
15. Kolb, V. A., Makeyev, E. V., Ward, W. W., and Spirin, A. S. (1996). Synthesis and maturation of green fluorescent protein in a cell-free translation system. Biotechnology Letters 18, 1447-1452.
16. Lakowicz, J. R., and Weber, G. (1973a). Quenching of fluorescence by oxygen. A probe for structural fluctuations in macromolecules. Biochemistry 12, 4161-4170.
17. Lakowicz, J. R., and Weber, G. (1973b). Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale. Biochemistry 12, 4171-4179.
18. Levine, L. D., and Ward, W. W. (1982). Isolation and characterization of a photoprotein, "Phialidin," and a spectrally unique green fluorescent protein from the bioluminescent jellyfish, Phialidium gregarium. Comp. Biochem. Physiol. 72B, 77-85.
19. Lossau, H., Kummer, A., Heinecke, R., Pöllinger-Dammer, F., Kompa, C., Bieser, G., Jonsson, T., Silva, C. M., Yang, M. M., Youvan, D. C., Michel-Beyerle, M. E. (1996). Time-resolved spectroscopy of wild-type and mutant green fluorescent proteins reveals excited state deprotonation consistent with fluorophore-protein interactions. Chem. Phys. 213, 1-16.
20. Moerner, W. E. (1977). Those blinking molecules. Science 277, 1059-1060.
21. Morise, H., Shimomura, O., Johnson, F. H., and Winant, J. (1996). Intermolecular energy transfer in the bioluminescent system of Aequorea. Biochemistry 13, 2656-2662.
22. Morin, J. G., and Hastings, J. W. (1971a). Biochemistry of the bioluminescence of colonial hydroids and other coelenterates. J. Cell. Physiol. 77, 305-312.
23. Morin, J. G., and Hastings, J. W. (1971b). Energy transfer in a bioluminescent system. J. Cell Physiol. 77, 313-318.
24. Ormö, M., Cubitt, A. B., Kallio, K., Gross, L. A., Rsien, R. Y. and Remington, S. J. (1996). Crystal structure of the Aequorea victoria green fluorescent protein. Science 273, 1392-1395.
25. 15N chemical shifts in a protein-DNA complex resulting from magnetic ordering in solution. J. Am. Chem. Soc. 119, 9825-9830.
26. Palm, G. J., Zdanov, A., Gaitanaris, G. A., Stauber, R., Pavlakis, G. N., and Wlodawer, A. (1997). The structural basis for spectral variations in green fluorescent protein. Nat. Struct. Biol. 4, 361-365.
27. Perozzo, M. A., Ward, K. B., Thompson, R. B., and Ward, W. W. (1988). X-ray diffraction and time-resolved fluorescence analysis of Aequorea green fluorescent protein crystals. J. Biol. Chem. 263, 7713-7716.
28. 2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc. Natl. Acad. Sci. 94, 12366-12371.
29. Prasher, D. C., Eckenrode, V. K., Ward, W. W., Prendergast, F. G., and Cormier, M. J. (1992). Primary structure of the Aequorea victoria green fluorescent protein. Gene 111, 229-233.
30. Shimomura, O. (1979). Structure of the chromophore of Aequorea green fluorescent protein. FEBS Lett. 104, 220-222.
31. Shimomura, O., and Johnson, F. H. (1975). Chemical nature of bioluminescence systems in coelenterates. Proc. Natl. Acad. Sci. U. S. A. 72, 1546-1549.
32. Sosnick, T. R., Mayne, L., Hiller, R., Englander, S. W. (1994). The barriers in protein folding. Nat. Struct. Biol. 1, 149-156.
33. Vander Bout, D. A., Yip, W.-T., Hu, D., Fu, D.-K., Swager, T. M., Barbara, P. F. (1997). Discrete intensity jumps and intermolecular electronic energy transfer in the spectroscopy of single conjugated polymer molecules. Science 277, 1076-1997.
34. Ward, W. W., and Bekman, S. H. (1982). Reversible denaturation of Aequorea green fluorescent protein: physical separation and characterization of the renatured protein. Biochemistry 21, 4535-4540.
35. Ward, W. W., and Cormier, M. J. (1978). Energy transfer via protein-protein interaction in Renilla bioluminescence. Photochem. Photobiol. 27, 389-396.
36. Ward, W. W., and Cormier, M. J. (1979). An energy transfer protein in coelenterate bioluminescence characterization of the Renilla green fluorescent protein (GFP). J. Biol. Chem. 254, 781-788.
37. Ward, W. W., Prentice, H. J., Roth, A. F., Cody, C. W., and Reever, S. C. (1982). Spectral perturbations of the Aequorea green fluorescent protein. Photochem. Photobiol. 35, 803-808.
38. Yang, F., Moss, L. G., and Phillips, G. M. (1996). The molecular structure of green fluorescent protein. Nat. Biotech. 14, 1246-1252.
39. Youvan, D. C., and Larrick, J. W. (1996). Fluorescent proteins and applications. Gene 173, 1-117.