Irreversible unfolding of the neutral pH form of influenza hemagglutinin demonstrates that it is not in a metastable state

Biochemistry

Volumn 42, Issue 17, 2003, Pages 5052-5057

  Epand, Raquel F ^a   Epand, Richard M ^a  

^a MCMASTER UNIVERSITY MEDICAL CENTRE   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

CIRCULAR DICHROISM;

ACTIVATION ENERGY; DIFFERENTIAL SCANNING CALORIMETRY; ENTHALPY; LIGHT SCATTERING; LIPIDS; PH EFFECTS; PROTEINS; THERMODYNAMIC STABILITY; THERMODYNAMICS; VIRUSES;

DISEASES;

DIOLEOYLPHOSPHATIDYLCHOLINE; GANGLIOSIDE GD 1A; HEMAGGLUTININ; LIPOSOME;

ARTICLE; CIRCULAR DICHROISM; DIFFERENTIAL SCANNING CALORIMETRY; ENERGY; INFLUENZA VIRUS; LIGHT SCATTERING; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; TEMPERATURE DEPENDENCE; THERMODYNAMICS; THERMOSTABILITY; VIRUS INHIBITION; VIRUS PARTICLE;

CALORIMETRY, DIFFERENTIAL SCANNING; DRUG STABILITY; HEMAGGLUTININ GLYCOPROTEINS, INFLUENZA VIRUS; HYDROGEN-ION CONCENTRATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; THERMODYNAMICS;

INFLUENZA VIRUS; RNA VIRUSES;

EID: 0038752634     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi034094b     Document Type: Article

References (27)

1. Blumenthal, R., Clauge, M. J., Durell, S. R., and Epand, R. M. (2003) Chem. Rev. 103, 53-70.
2. Wilson, I. A., Skehel, J. J., and Wiley, D. C. (1981) Nature 289, 366-373.
3. Bullough, P. A., Hughson, F. M., Skehel, J. J., and Wiley, D. C. (1994) Nature 377, 37-43.
4. Carr, C. M., and Kim, P. S. (1993) Cell 73, 823-832.
5. Carr, C. M., Chaudhry, C., and Kim, P. S. (1997) Proc. Natl. Acad. Sci. U.S.A. 94, 14306-14313.
6. Remeta, D. P., Krumbiegel, M., Minetti, C. A., Puri, A., Ginsburg, A., and Blumenthal, R. (2002) Biochemistry 41, 2044-2054.
7. Epand, R. M., and Epand, R. F. (2002) Biochem. J. 365, 841-848.
8. Lepock, J. R., Ritchie, K. P., Kolios, M. C., Rodahl, A. M., Heinz, K. A., and Kruuv, J. (1992) Biochemistry 31, 12706-12712.
9. Kurganov, B. I., Lyubarev, A. E., Sanchez-Ruiz, J. M., and Shnyrov, V. L. (1997) Biophys. Chem. 69, 125-135.
10. Sanchez-Ruiz, J. M., Lopez-Lacomba, J. L., Cortijo, M., and Mateo, P. L. (1988) Biochemistry 27, 1648-1652.
11. Suzuki, Y. (1994) Prog. Lipid Res. 33, 429-457.
12. Oxford, J. S., Corcoran, T., and Hugentobler, A. L. (1981) J. Biol. Stand. 9, 483-491.
13. Ruigrok, R. W., Martin, S. R., Wharton, S. A., Skehel, J. J., Bayley, P. M., and Wiley, D. C. (1986) Virology 155, 484-497.
14. Cusack, S., Ruigrok, R. W., Krygsman, P. C., and Mellema, J. E. (1985) J. Mol. Biol. 186, 565-582.
15. Booy, F. P., Ruigrok, R. W., and van Bruggen, E. F. (1985) J. Mol. Biol. 184, 667-676.
16. Nir, S., Stegmann, T., and Wilschut, J. (1986) Biochemistry 25, 257-266.
17. Wharton, S. A., Ruigrok, R. W., Martin, S. R., Skehel, J. J., Bayley, P. M., Weis, W., and Wiley, D. C. (1988) J. Biol. Chem. 263, 4474-4480.
18. Korte, T., Ludwig, K., Krumbiegel, M., Zirwer, D., Damaschun, G., and Herrmann, A. (1997) J. Biol. Chem. 272, 9764-9770.
19. Huang, Q., Opitz, R., Knapp, E. W., and Herrmann, A. (2002) Biophys. J. 82, 1050-1058.
20. Ghosh, J. K., Peisajovich, S. G., and Shai, Y. (2000) Biochemistry 39, 11581-11592.
21. Shai, Y. (2000) Biosci. Rep, 20, 535-555.
22. Haltia, T., and Freire, E. (1995) Biochim. Biophys. Acta 1241, 295-322.
23. Loladze, V. V., Ermolenko, D. N., and Makhatadze, G. I. (2001) Protein Sci. 10, 1343-1352.
24. Makhatadze, G. I., and Privalov, P. L. (1995) Adv. Protein Chem. 47, 307-425.
25. Robertson, A. D., and Murphy, K. P. (1997) Chem. Rev. 97, 1251-1267.
26. Wharton, S. A., Skehel, J. J., and Wiley, D. C. (1986) Virology 149, 27-35.
27. Nebel, S., Bartoldus, I., and Stegmann, T. (1995) Biochemistry 34, 5705-5711.