Direct energy transfer to study the 3D structure of non-native proteins: AGH complex in molten globule state of apomyoglobin

Protein Engineering

Volumn 12, Issue 6, 1999, Pages 485-490

  Tcherkasskaya, Olga ^a,b   Ptitsyn, Oleg B ^a,c  

^a NATIONAL CANCER INSTITUTE   (United States)

^b INSTITUTE OF MACROMOLECULAR COMPOUNDS   (Russian Federation)

^c INSTITUTE OF PROTEIN RESEARCH   (Russian Federation)

Author keywords

Apomyoglobin; Direct energy transfer; Fluorescence; Molten globule

Indexed keywords

3 NITROTYROSINE; MYOGLOBIN; TRYPTOPHAN;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; ENERGY TRANSFER; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN LOCALIZATION; PROTEIN STRUCTURE;

EID: 0033035790     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/12.6.485     Document Type: Article

References (35)

1. Baldwin, R.L. (1993) Curr. Opin. Struct. Biol., 3, 84-91.
2. Baum, J., Dobson, C.M., Evans, P.A. and Hanly, C. (1989) Biochemistry, 28, 7-13.
3. Blumen, A. (1980) J. Chem. Phys., 74, 6926-6933.
4. Borkman, R.A. and Phillips, S.R. (1985) Exp. Eye Res., 40, 819-826.
5. Bychkova, V.E. and Ptitsyn, O.B. (1993) Chemtracts Biochem. Mol. Biol., 4, 133-163.
6. Bychkova, V.E. and Ptitsyn, O.B. (1995) FEBS Lett., 359, 6-8.
7. Cheung, H.C. (1991) In Lakowicz, J.R. (ed.), Topics in Fluorescence Spectroscopy, Vol. 2. Plenum Press, New York, pp. 127-176, and references cited therein.
8. Eisinger, M. (1969) J. Photochem. Photobiol., 9, 247-258.
9. Eliezer, D., Yao, J., Dyson, H.J. and Wright, P.E. (1998) Nature Struct. Biol., 5, 148-155.
10. Evans, S.V. and Brayer, G.D. (1988) J. Biol. Chem., 263, 4263-4268.
11. Evans, S.V. and Brayer, G.D. (1990) J. Mol. Biol., 213, 885-897.
12. Ewbank, J.J. and Creighton, T.E. (1991) Nature, 350, 518-520.
13. Förster, T. (1948) Ann. Phys., 2, 55-75.
14. Goto, Yu. and Fink, A.L. (1990) J. Mol. Biol., 214, 803-805.
15. Hochstrasser, R.M. and Johnson, C.K. (1993) In Kaiser, W. (ed.), Topics in Applied Physics, 2nd edn, Vol. 60. Springer, Berlin, pp. 368-372.
16. Hughson, F.M., Wright, P.E. and Baldwin, R.L. (1990) Science 249, 1544-1548.
17. Irace, G., Balestrieri, C., Parlato, G., Servillo, L. and Colonna, G. (1981) Biochemistry, 20, 792-799.
18. Jeng, M.-F., Englander, S.W., Elöve, G.A., Wand, A.J. and Roder, H. (1990) Biochemistry, 29, 10433-10437.
19. Jennings, P.A. and Wright, P.E. (1990) Science, 262, 892-896.
20. Kataoka, M., Nishii, I., Fujisawa, T., Ueki, T., Tokunaga, F. and Goto, Yu. (1995) J. Mol. Biol., 249, 215-228.
21. Laemmli, U.K. (1970) Nature, 227, 680-685.
22. Lakowicz, J.R. (1983) Principles of Fluorescence Spectroscopy. Plenum Press, New York, pp. 303-339, and references cited therein.
23. Lundblad, R.L. (1991) Chemical Reagents for Protein Modification. CRC Press, Boca Raton, FL, pp. 239-266, and references cited therein.
24. Peng, Z.-Y. and Kim, P.S. (1994) Biochemistry, 33, 2136-2141.
25. Postnikova, G.V., Komarov, Yu. E. and Yumakova, E.M. (1991) Eur. J. Biochem., 198, 223-232.
26. Ptitsyn, O.B. (1973) Dokl. Akad. Nauk SSSR, 210, 1213-1215.
27. Ptitsyn, O.B. (1995) Adv. Protein Chem., 47, 83-229.
28. Redford, S.E., Dobson, C.M. and Evans, P.A. (1992) Nature, 358, 302-307.
29. Riordan, J.F., Sokolovsky, J.F. and Vallee, B.L. (1967) Biochemistry, 6, 358-361.
30. Rischel, C. and Poulsen, F.M. (1995) FEBS Lett., 374, 105-109.
31. Rischel, C., Thyberg, P., Rigler, R. and Poulsen, F.M. (1996) J. Mol. Biol., 257, 877-885.
32. Roder, H., Elöve, G.A. and Englander, S.W. (1988) Nature, 335, 700-704.
33. Teale, F.W.J. (1959) Biochim. Biophys. Acta, 35, 543.
34. Wu, L.C., Peng, Z.-Y. and Kim, P.S. (1995) Nature Struct. Biol., 2, 281-285.
35. Zhang, B. and Peng, Z.-Y. (1996) J. Biomol. Chem., 271, 28734-28737.