Pea lectin in alkaline conditions: Formation of molten globule-like intermediate and its structural and thermal studies under the influence of hexafluoroisopropanol

Protein and Peptide Letters

Volumn 15, Issue 6, 2008, Pages 606-611

  Naseem, Farah ^a   Khan, Rizwan Hasan ^a  

^a ALIGARH MUSLIM UNIVERSITY   (India)

Author keywords

Alkaline unfolding; HFIP induced state; MG like state; Pea lectin

Indexed keywords

HEXAFLUORO 2 PROPANOL; PEA LECTIN; PLANT LECTIN; PROPANOL;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; CIRCULAR DICHROISM; DRUG EFFECT; MOLECULAR GENETICS; PH; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; TEMPERATURE;

AMINO ACID SEQUENCE; CIRCULAR DICHROISM; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; PLANT LECTINS; PROPANOLS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; TEMPERATURE;

PISUM SATIVUM;

EID: 47249084756     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986608784966868     Document Type: Article

References (26)

1. Dili, K. A. and Shortle, D. (1991) Ann. Rev. Biochem., 60, 795.
2. Shortle, D. (1993) Curr. Opin. Struct. Biol., 3, 66.
3. Bychkova, V.E., Dujsekina, A.E., Klenin, S.I., Tiktopulo, E.I., Uversky, V.N. and Ptitsyn, O.B. (1996) Biochemistry, 35, 6058.
4. Lu, H., Buck, M., Radford, S.E. and Dobson, CM. (1997) J. Mol. Biol., 265, 112.
5. Chiti, F., Taddei, N., Webster, P., Hamada, D., Fiaschi, T., Ramponi, G. and Dobson, CM. (1999) Nat. Struct. Biol., 6, 380.
6. Mchaourab, H.S., Hyde, J.S. and Fex, J.B. (1993) Biochemistry; 32, 11895.
7. Cort, J., Liu, Z., Lee, G., Harris, S.M., Prickett, K.S., Gaeta, L.S. and Andersen, N.H. (1994) Biochem. Biophys. Res. Commun., 204, 1088.
8. Nelson, J.W. and Kallenbach, N.R. (1986) Proteins Struct. Funct. Genet., 1, 211.
9. Nelson, J.W. and Kallenbach, N.R. (1989) Biochemistr., 28, 5256.
10. Shiraki, K., Nishikawa, K. and Goto, Y. (1995) J. Mol. Biol., 245, 180.
11. Hamada, D., Kuroda, Y., Tanaka, T. and Goto, Y. (1995) J. Mol. Biol., 254, 737.
12. Lis, H. and Sharon, N. (1991) Curr. Opin. Struct. Biol.,1, 741.
13. Brewer, C.F. (1996) Chemtracts-Biochem., 6, 165.
14. Einspahr, H., Parks, E.H., Suguna, K., Subramanian, E. and Suddath, F.L. (1986) J. BioL Chem., 261, 16518.
15. Naseem, F. and Khan, R.H. (2005) Biochim. Biophys. Acta., 1723, 192.
16. Agarwal, B.B. and Goldstein, I.J. (1967) Biochim. Biophys. Acta, 147, 262-271.
17. Bhattacharya, L., Brewer, C.F., Brown, R.D. and Koenig, S.H. (1985) Biochemistry, 24, 4974.
18. Lowry, O.H., Rosebrough, N.J., Farr, A.L. and Randall, R.J. (1951) J. Biol. Chem., 193, 265.
19. Kay, M.S. and Baldwin, R.L. (1996) Nat. Struct. Biol., 3, 439.
20. Song, J., Bai, P., Luo, L. and Peng, Z.Y. (1998) J. Mol. Biol., 280, 167.
21. Wu, L.C. and Kim, P.S. (1998) J. Mol. Biol., 280, 175.
22. Shortle, D. and Ackerman, M.S. (2001) Science, 293,487.
23. Nozaki, Y. and Tanford, C. J. (1971) Biol. Chem., 246, 2211.
24. Thomas, P.D. and Dill, K.A. (1993) Protein Sci., 2, 2050.
25. Liu, Y. and Bolen, D.W. (1995) Biochemistry, 34, 12884.
26. Molina, M.I., Petrucceili, S. and Anon, M.C. (2004) J. Agric. Food Chem., 52, 6023.