Secondary structure and oligomerization behavior of equilibrium unfolding intermediates of the λ Cro repressor

Biochemistry

Volumn 38, Issue 17, 1999, Pages 5633-5642

  Fabian, Heinz ^a   Fälber, Katja ^a   Gast, Klaus ^a   Reinstädler, Diane ^b   Rogov, Vladimir V ^c,d   Naumann, Dieter ^b   Zamyatkin, Dmitry F ^c   Filimonov, Vladimir V ^c  

^a MAX DELBRÜCK CENTER FOR MOLECULAR MEDICINE   (Germany)

^b ROBERT KOCH INSTITUTE   (Germany)

^c INSTITUTE OF PROTEIN RESEARCH   (Russian Federation)

^d GOETHE UNIVERSITY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

REPRESSOR PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; HYDROGEN BOND; MOLECULAR INTERACTION; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE;

AMINO ACID SUBSTITUTION; BACTERIOPHAGE LAMBDA; CROSS-LINKING REAGENTS; CYANOGEN BROMIDE; DIFFUSION; DNA-BINDING PROTEINS; HEAT; LIGHT; MOLECULAR WEIGHT; PEPTIDE FRAGMENTS; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; REPRESSOR PROTEINS; SCATTERING, RADIATION; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; VALINE; VIRAL PROTEINS;

EID: 0039129406     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi982120d     Document Type: Article

References (39)

1. Privalov, P. L. (1996) J. Mol. Biol. 258, 707-725.
2. Baldwin, R. L. (1997) Nat. Struct. Biol. 4, 965-966.
3. Kuwajima, K. (1989) Proteins: Struct., Funct., Genet. 6, 87-103.
4. Dobson, C. M. (1992) Curr. Opin. Struct. Biol. 2, 6-12.
5. Johnson, A., Meyer, B. J., and Ptashne, M. (1978) Proc. Natl. Acad. Sci. U.S.A. 75, 1783-1787.
6. Anderson, W. F., Ohlendorf, D. H., Takeda, Y., and Mathews, B. W. (1981) Nature 290, 754-758.
7. Weber, P. L., Wemmer, D. E., and Reid, B. R. (1985) Biochemistry 24, 4553-4562.
8. Matsuo, H., Shirakawa, M., and Kyogoku, Y. (1995) J. Mol. Biol. 254, 668-680.
9. Bolotina, I. A., Kurochkin, A. V., and Kirpichnikov, M. P. (1993) FEBS Lett. 155, 291-294.
10. Pakula, A. A., and Sauer, R. T. (1989) Proteins: Struct., Funct., Genet. 5, 202-210.
11. Mossing, M. C., and Sauer, R. T. (1990) Science 250, 1712-1715.
12. Hubbard, A. J., Bracco, L. P., Eisenbeis, S. J., Gayle, R. B., Beaton, G., and Caruthers, M. H. (1990) Biochemistry 29, 9241-9249.
13. Albright, R. A., Mossing, M. C., and Mathews, B. W. (1996) Biochemistry 35, 735-742.
14. Mollah, A. K. M. M., Alema, M. A., Albright, R. A., and Mossing, M. C. (1996) Biochemistry 35, 743-748.
15. Shirakawa, M., Hiroshi, M., and Kyogoku, Y. (1991) Protein Eng. 4, 545-552.
16. Baleja, J. D., and Sykes, B. D. (1994) Biochem. Cell Biol. 72, 95-108.
17. Gitelson, G. I., Griko, Y. V., Kurochkin, A. V., Rogov, V. V., Kutychenko, V. P., Kirpichnikov, M. P., and Privalov, P. L. (1991) FEBS Lett. 289, 201-204.
18. Griko, Y. V., Rogov, V. V., and Privalov, P. L. (1992) Biochemistry 31, 12701-12705.
19. Filimonov, V. V., and Rogov, V. V. (1996) J. Mol. Biol. 255, 767-777.
20. Harrison, P. M., Bamborough, P., Daggett, V., Prusiner, S. B., and Cohen, F. E. (1997) Curr. Opin. Struct. Biol. 7, 53-59.
21. Kelly, L. W. (1998) Curr. Opin. Struct. Biol. 8, 101-106.
22. Fabian, H., Schultz, C., Backmann, J., Hahn, U., Saenger, W., Mantsch, H. H., and Naumann, D. (1994) Biochemistry 33, 10725-10730.
23. Reinstädler, D., Fabian, H., Backmann, J., and Naumann, D. (1996) Biochemistry 35, 15822-15830.
24. Gast, K., Damaschun, G., Damaschun. H., Misselwitz, R., and Zirwer, D. (1993) Biochemistry 32, 7747-7752.
25. Gast, K., Nöppert, A., Müller-Frohne, M., Zirwer, D., and Damaschun, G. (1997) Eur. Biophys. J. 25, 211-219.
26. Rogov, V. V., and Griko, Yu. V. (1993) Mol. Biol. (USSR) 27, 798-804.
27. Fabian, H., Schultz, C., Naumann, D., Landt, O., Hahn, U., and Saenger, W. (1993) J. Mol. Biol. 232, 967-981.
28. Mantsch, H. H., Moffatt, D. J., and Casal, H. L. (1988) J. Mol. Struct. 173, 285-298.
29. Gast, K., Damaschun, G., Misselwitz, R., and Zirwer, D. (1992) Eur. Biophys. J. 21, 357-362.
30. Provencher, S. W. (1982) Comp. Phys. Commun. 27, 229-242.
31. Schmidt, M. (1993) in Dynamic Light Scattering. The method and some applications (Brown, W., Ed.) pp 372-406, Clarendon Press, Oxford.
32. Chirgadze, Y. N., Fedorov, O. V., and Trushina, N. P. (1975) Biopolymers 14, 679-694.
33. Blout, E. R., de Loze, C., and Asadourian, A. (1961) J. Am. Chem. Soc. 83, 1895-1900.
34. Backmann, J., Schultz, C., Fabian, H., Hahn, U., Saenger, W., and Naumann, D. (1996) Proteins: Struct., Funct., Genet. 24, 379-387.
35. Jackson, M., and Mantsch, H. H. (1995) Crit. Rev. Biochem. Mol. Biol. 30, 95-120.
36. Krimm, S., and Bandekar, J. (1986) Adv. Protein Chem. 38, 181-364.
37. Fabian, H., and Mantsch, H. H. (1995) Biochemistry 34, 13651-13655.
38. Reisdorf, W. C., and Krimm, S. (1996) Biochemistry 35, 1383-1386.
39. Garcia Bernal, J. M., and Garcia de la Torre, J. (1981) Biopolymers 20, 129-139.