Measurement of intrinsic fluorescence to probe the conformational flexibility and thermodynamic stability of a single tryptophan protein entrapped in a sol-gel derived glass matrix

Analyst

Volumn 123, Issue 8, 1998, Pages 1735-1744

  Zheng, Lui ^a   Brennan, John D ^a  

^a BROCK UNIVERSITY   (Canada)

Author keywords

Biosensor; Fluorescence; Protein; Sol gel; Stability

Indexed keywords

ACRYLAMIDE; GUANIDINE; MONELLIN; PROTEIN; TRYPTOPHAN;

ANALYTIC METHOD; ANISOTROPY; ARTICLE; CONTROLLED STUDY; ENCAPSULATION; FLUORESCENCE ANALYSIS; GEL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN STABILITY;

EID: 0031655462     PISSN: 00032654     EISSN: None     Source Type: Journal    
DOI: 10.1039/a800710a     Document Type: Article

References (50)

1. Braun, S., Rappoport, S., Zusman, R., Avnir, D., and Ottolenghi, M., Mater. Lett., 1990, 10, 1.
2. (a) Nishida, F., McKiernan, J. M., Dunn, B., Zink, J. I., Brinker, C. J., and Hurd, A. J., J. Am. Ceram. Soc., 1995, 78, 1640;
3. (b) Ellerby, L. M., Nishida, C. R., Nishida, F., Yamanaka, S. A., Dunn, B., Valentine, J. S., and Zink, J. I., Science, 1992, 255, 1113.
4. (a) Dave, B. C., Dunn, B., Valentine, J. S., and Zink, J. I., Anal. Chem., 1994, 66, 1120A;
5. (b) Avnir, D., Braun, S., Lev, O., and Ottolenghi, M., Chem. Mater., 1994, 6, 1605;
6. (c) Yamanaka, S. A., Dunn, B., Valentine, J. S., and Zink, J. I., J. Am. Chem. Soc., 1995, 117, 9095.
7. (a) Braun, S., Rappoport, S., Zusman, R., Shteltzer, S., Drukman, S., Avnir, D., and Ottolenghi, M., in Biotechnology: Bridging Research and Applications, ed. Kamely, D., Chakrobary, A., and Kornguth, S. E., Kluwer Academic Publishers, Amsterdam, 1991, p. 205;
8. (b) Heichal-Segai, O., Rappoport, S., and Braun, S., Biotechnology, 1995, 13, 798;
9. (d) Reetz, M. T., Zonta, A., and Simpelkamp, J., Angew. Chem., Int. Ed. Engl., 1995, 34, 301.
10. (a) Dave, B. C., Soyez, H., Miller, J. M., Dunn, B., Valentine, J. S., and Zink, J. I., Chem. Mater., 1995, 7, 1431;
11. (b) Jordan, J. D., Dunbar, R. A., and Bright, F. V., Anal. Chem., 1995, 67, 2436.
12. (a) Narang, U., Jordan, J. D., Bright, F. V., and Prasad, P. N., J. Phys. Chem., 1994, 98, 8101;
13. (b) Narana, U., Bright, F. V., and Prasad, P. N., Appl. Spectrosc., 1993, 47, 229;
14. (c) Matsui, K., Matsuzuka, T., and Fujita, H., J. Phys. Chem., 1989, 93, 4991.
15. Eftink, M. R., in Methods of Biochemical Analysis: Protein Structure Determination, ed. Suelter, C. H., Wiley, New York, 1991, vol. 35, pp. 127-206.
16. (a) Dahms, T. E. S., Willis, K. J., and Szabo, A. G., J. Am. Chem. Soc., 1995, 117, 2321;
17. (b) Dahms, T. E. S., and Szabo, A. G., Biophys. J., 1995, 69, 569.
18. Demchenko, A. P., Gryczynski, I., Gryczynski, Z., Wiczk, W., Malak, H., and Fishman, M., Biophys. Chem., 1993, 48, 39.
19. Hargrove, M. S., Krzywda, S., Wilkinson, A. J., Dou, Y., Ikeda-Saito, M., and Olson, J. S., Biochemistry, 1994, 33, 11 767.
20. Eftink, M. R., Biophys. J., 1994, 66, 482.
21. Beechem, J. M., Proc. SPIE, 1992, 1640, 676.
22. Zheng, L., Reid, W. R., and Brennan, J. D., Anal. Chem., 1997, 69, 3940.
23. (a) Edmiston, P. L., Wambolt, C. L., Smith, M. K., and Saavedra, S. S., J. Colloid Interface Sci., 1994, 163, 395;
24. (b) Wambolt, C. L., and Saavedra, S. S., J. Sol-Gel Sci. Tech., 1996, 7, 53.
25. (a) Morris, J., and Cagan, R. H., Biochim. Biophys. Acta, 1972, 261, 114;
26. (b) Van der Wel, H., FEBS Lett., 1972, 21, 88.
27. Van der Wel, H., and Loeve, K., FEBS Lett., 1973, 29, 181.
28. (a) Ogata, C., Hatada, M., Tomlinson, G., Shin, W.-C., and Kim, S.-H., Nature (London), 1987, 328, 739;
29. (b) Somoza, J. R., Jiang, F., Liang, T., Rang, C.-H., Cho, J. M., and Kim, S.-H., J. Mol. Biol., 1993, 234, 390.
30. Brand, J. G., and Cagan, R. H., Biochim. Biophys. Acta, 1977, 493, 178.
31. Pace, C. N., Shirley, B. A., and Thomson, J. A., in Protein Structure and Function: A Practical Approach, ed. Chreighton, T. E., IRL Press Oxford, 1989, pp. 311-330.
32. Santoro, M. M., and Bolen, D. W., Biochemistry, 1988, 27, 8063.
33. (a) Eftink, M. R., and Ghiron, C. A., Biochemistry, 1976, 15, 672;
34. (b) Eftink, M. R., and Ghiron, C. A., Biochemistry, 1977, 16, 5546;
35. (c) Eftink, M. R., and Ghiron, C. A., Biochim. Biophys. Acta, 1987, 916, 343.
36. (a) Xu, S., Ballard, L., Kim, Y. J., and Jonas, J., J. Phys. Chem., 1995, 99, 5787;
37. (b) Korb, J.-P., Delville, A., Xu, S., Demeulenaere, G., Costa, P., and Johas, J., J. Chem. Phys., 1994, 101, 7074;
38. (c) Shen, C., and Kostic, N. M., J. Am. Chem. Soc., 1997, 119, 1304.
39. Lakowicz, J. R., and Weber, G., Biochemistry, 1973, 18, 4161.
40. Kirby, E. P., and Steiner, R. F., J. Phys. Chem., 1970, 74, 4480.
41. Lakowicz, J. R., Principles of Fluorescence Spectroscopy, Plenum Press, New York, 1983, pp. 129-134.
42. Liu, Y., and Bolen, D. W., Biochemistry; 1995, 34, 12 884.
43. Privolov, P. L., Annu. Rev. Biophys. Chem., 1989, 18, 47.
44. Eftink, M. R., Ghiron, C. A., Kautz, R. A., and Fox, R. O., Biochemistry, 1991, 30, 1193.
45. Privolov, P. L., and Khechinashvili, N. N., J. Mol. Biol, 1974, 86, 665.
46. (a) Brinker, C. J., and Scherer, G. W., Sol-Gel Science, Academic Press, New York, 1989;
47. (b) Hench, L. L., and West, J. K., Chem. Rev., 1990, 90, 33.
48. Pace, C. N., Laurents, D. V., and Thomson, J. A., Biochemistry, 1990, 29, 2564.
49. Lehrer, S. S., Biochemistry, 1971, 10, 3254.
50. Lundgren, J. S., Heitz, M. P., and Bright, F. V., Anal. Chem., 1995, 67, 3775.