Time-resolved fluorescence study of the single tryptophans of engineered skeletal muscle troponin C

Biophysical Journal

Volumn 73, Issue 2, 1997, Pages 1042-1055

  She, Mingda ^a   Dong, Wen Ji ^b   Umeda, Patrick K ^c   Cheung, Herbert C ^a,b  

^a UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

^b UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

^c University of Alabama at Birmingham   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

TRYPTOPHAN;

ANISOTROPY; ARTICLE; DRUG RECEPTOR BINDING; FLUORESCENCE; GENETIC ENGINEERING; HYDRODYNAMICS; NONHUMAN; PROTEIN DOMAIN; RADIOISOTOPE DECAY; SKELETAL MUSCLE;

GALLUS GALLUS;

EID: 0030749604     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78137-2     Document Type: Article

References (45)

1. Bakhshiev, N., G. Yu, T. Mazuerenko, and I. V. Piterskaya. 1966. Luminescence decay in different portions of the luminescence spectrum of molecules in viscous solution. Opt. Spectrosc. 21:307-309.
2. Chabbert, M., T. J. Lukas, D. M. Watterson, P. H. Auxelsen, and F. G. Prendergast. 1991. Fluorescence analysis of calmodulin mutants containing tryptophan: conformational changes induced by calmodulin-binding peptides from myosin light chain kinase and protein kinase II Biochemistry. 30:7615-7639.
3. Cheung, H. C., C.-K. Wang, and N. A. Malik. 1987. Interaction of troponin subunits: free energy of binary and ternary complexes. Biochemistry 26:5904-5907.
4. Clark, I. D., and A. G. Szabo. 1993. A time-resolved fluorescence study of TnC single tryptophan mutant, F29W. Biophys. J. 64:135a. (Abstr.).
5. Dahms, T. E. S., K. J. Willis, and A. G. Szabo. 1993. Fluorescence decay kinetics of a tryptophanyl residue in a protein crystal. Biophys. J. 64:55a. (Abstr.).
6. Davis, D. M., D. McLoskey, D. J. Birch, R. M. Swart, P. R. Gellert, and R. S. Kittlety. 1994. Fluorescence studies of tryptophan and human serum albumin (HSA) in AOT reverse micelles. SPIE PROC 2137: 331-324.
7. DeToma, R. P., J. H. Easter, and L. Brand. 1976. Dynamic interactions of fluorescence probes with the solvent environment. J. Am. Chem. Soc. 98:5001-5007.
8. Donzel, B., P. Gauduchon, and Ph. Wahl. 1974. Study of the conformation in the excited state of two tryptophanyl diketopiperazines. J. Am. Chem. Soc. 96:801-808.
9. Eftink, M. R. 1991. Fluorescence quenching: theory and applications, In Topics in Fluorescence Spectroscopy, Vol. 2. J. R. Lakowicz, editor. Plenum Press, New York. 53-126.
10. Eftink, M. R., and C. A. Ghiron. 1976. Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies. Biochemistry. 15:672-680.
11. Fabiato, A. 1988. Computer programs for calculating total from specified free and free from total ionic concentrations in aqueous solutions containing multiple metals and ligands. Methods Enzymol. 157:378-417.
12. Grinvald, A., and I. Z. Steinberg. 1974. On the analysis of fluorescence decay kinetics by the method of least-squares. Anal. Biochem. 59: 583-589.
13. Heidorn, D. B., and J. Trewhella. 1988. Comparison of the crystal and solution structures of calmodulin and troponin C. Biochemistry. 27: 909-915.
14. Herzberg, O., and M. N. G. James. 1985. Structure of the calcium regulatory protein troponin-C at 2.8 Å resolution. Nature. 313:653-659.
15. 2+-induced conformational transition of troponin C. J. Biol. Chem. 261:2638-2644.
16. Howarth, J. W., G. A. Krudy, X. Lin, J. A. Putkey, and R. Rosevear. 1995. An NMR spin-labeled study of the effects of binding calcium and troponin I inhibitory peptide to cardiac troponin C. Protein Sci. 4:671-680.
17. Hubbard, S. R., K. D. Hodgson, and S. Doniach. 1988. Small-angle x-ray scattering investigation of the solution structure of troponin C. J. Biol. Chem. 263:4151-4158.
18. Kretsinger, R. H., and C. E. Nockolds. 1973. Carp muscle calcium-binding protein. Structure determination and general description. J. Mol. Biol. 248:3313-3326.
19. Lakowicz, J. R., and H. Cherek. 1980. Dipolar relaxation in proteins in the nanosecond time scale observed by wavelength-resolved phase fluorometry of tryptophan fluorescence. J. Biol. Chem. 255:831-834.
20. 2+ binding sites and interactions with troponin I and troponin T. J. Biol. Chem. 253:5452-5459.
21. Liao, R., C.-K. Wang, and H. C. Cheung. 1992. Time-resolved tryptophan emission study of cardiac troponin I. Biophys. J. 63:986-995.
22. Lipari, G., and A. Szabo. 1982. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromo ecules. 1. Theory and range of validity. J. Am. Chem. Soc. 104:4546-4558.
23. Mehler, E. L., J. L. Pascual-Ahuir, and H. Weinstein 1991. Structural dynamics of calmodulin and troponin C. Protein Sci. 4:625-637.
24. Parker, C. A., and W. T. Rees. 1960. Correction of fluorescence spectra and measurement of fluorescence quantum efficiency. Analyst (London). 85:587-600.
25. 2+ affinity. Biochemistry. 31:6545-6553.
26. Pearlstone, J. R., W. D. McCubbin, C. M. Kay, B. D. Sykes, and L. B. Smillie. 1992b. Spectroscopic analysis of a methionine-48 to tyrosine mutant of chicken troponin C. Biochemistry. 31:9703-9708.
27. Petrich, J. W., J. W. Longworth, and G. F. Fleming. 1987. Internal motion and electron transfer in proteins: a picosecond fluorescence study of three homologous azurins. Biochemistry. 26:2711-2722.
28. Philips, L. A., S. P. Webb, S. J. Martinez III, G. R. Fleming, and D. H. Levy. 1988. Time-resolved spectroscopy of tryptophan conformers in a supersonic jet. J. Am. Chem. Soc. 110:1352-1355.
29. Potter, J. D., and J. Gergely. 1975. The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar ATPase. J. Biol. Chem. 250:4628-4633.
30. 2]oxytocin. Biochemistry. 31:1585-1594.
31. She, M., W.-J. Dong, P. K. Umeda, and H. C. Cheung. 1997. Single-tryptophan mutants of troponin C from chicken skeletal muscle. An optical probe of the conformation of the regulatory domain. Euro. J. Biochem. In press.
32. She, M., P. K. Umeda, and H. C. Cheung. 1995. Intramolecular distances in troponin C mutants. Biophys. J. 68:58a. (Abstr.).
33. Strynadka, N. C. J., and M. N. G. James. 1989. Crystal structures of the helix-loop-helix calcium-binding proteins. Annu. Rev. Biochem. 58: 951-988.
34. Sundaralingam, M., R. Bergstrom, G. Strasburg, R. T. Rao, P. Roychowdhury, M. Greaser, and B. C. Wang. 1985. Molecular structure of troponin C from chicken skeletal muscle at 3-Å resolution. Science. 227:945-948.
35. Szabo, A. G., and D. M. Rayner. 1980. Fluorescence decay of tryptophan conformers in aqueous solution. J. Am. Chem. Soc. 102:554-563.
36. Tao, T., B-J. Gong, and P. C. Leavis. 1990. Calcium induced movement of troponin I relative to actin in skeletal muscle thin filaments. Science. 247:1339-1341.
37. Tilstra, L., M. C. Sattler, W. R. Cherry, and M. D. Barkley. 1990. Fluorescence of a nationally constrained tryptophan derivative, 3-carboxy-1,2,3,4-tetrahydro-2-carboline. J. Am. Chem. Soc. 112:9176-9182.
38. b excitation bands. Photochem. Photobiol. 25:441-444.
39. Van Gilst, M., C. Tang, A. Roth, and B. Hudson. 1994. Quenching interactions and nonexponential decay: tryptophan 138 of bacteriophage T4 lysozyme. J. Fluorescence. 4:203-208.
40. Wahl, Ph., and J. C. Auchet. 1972. Résolution des spectres de fluorescence au moyen des déclines. Application à l'étude de la sérum albumine. Biochim. Biophys. Acta. 285:99-117.
41. Wang, C.-K., J. Lebowitz, and H. C. Cheung. 1989. Acid-induced dimerization of skeletal troponin C. Protein. 6:424-430.
42. Wang, C.-K., R. Liao, and H. C. Cheung. 1993. Rotational dynamics of skeletal muscle troponin C. J. Biol. Chem. 268:16471-16477.
43. Ware, W. R., S. K. Lee, G. J. Brant, and P. P. Chow. 1971. Nanosecond time-resolved emission spectroscopy: spectral shifts due to solvent-excited solute relaxation. J. Chem. Phys. 54:4729-4737.
44. Werner, T. C., and L. S. Foster. 1979. The fluorescence of tryptophanyl peptides. Photochem. Photobiol. 29:905-914.
45. Yu, H.-T., W. J. Colucci, M. I. McLaughlin, and M. D. Barkley. 1992. Fluorescence quenching in indoles by excited-state proton transfer. J. Am. Chem. Soc. 114:8449-8454.