Unfolding and refolding of bovine β-lactoglobulin monitored by hydrogen exchange measurements

Journal of Molecular Biology

Volumn 293, Issue 4, 1999, Pages 953-969

  Ragona, L ^a   Fogolari, F ^c   Romagnoli, S ^c   Zetta, L ^a   Maubois, J L ^b   Molinari, H ^c  

^a CNR   (Italy)

^b CEMAGREF   (France)

^c UNIVERSITY OF VERONA   (Italy)

Author keywords

Bovine lactoglobulin; H 2H exchange; Nuclear magnetic resonance; Unfolding free energy; Urea unfolding and refolding

Indexed keywords

AMIDE; BETA LACTOGLOBULIN; HYDROGEN; PROTON; UREA;

AQUEOUS SOLUTION; ARTICLE; CATTLE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY;

BOS TAURUS; BOVINAE; CALYX;

EID: 0033527582     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3191     Document Type: Article

References (36)

1. Arai M., Ikura T., Semisotnov G. V., Kihara H., Amemiya Y., Kuwajima K. Kinetic refolding of β-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy. J. Mol. Biol. 275:1998;149-162.
2. Bai Y., Englander S. W. Future directions in folding: the multi-state nature of protein structure. Proteins: Struct. Funct. Genet. 24:1996;145-151.
3. Bai Y., Milne J. S., Mayne L., Englander S. W. Primary structure effects on peptide group hydrogen exchange. Proteins: Struct. Funct. Genet. 17:1993;75-86.
4. Bai Y., Milne J. S., Mayne L., Englander S. W. Protein stability parameters measured by hydrogen exchange. Proteins: Struct. Funct. Genet. 20:1994;4-14.
5. Bai Y., Sosnick T. R., Mayne L., Englander S. W. Protein folding intermediates: native state hydrogen exchange. Science. 269:1995;192-197.
6. Bartels C., Xia T., Billeter M., Güntert P., Wüthrich K. The program XEASY for computers-supported NMR spectra analysis of biological macromolecules. J. Biomol. NMR. 5:1995;1-10.
7. Bax A., Davis D. G. MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65:1985;355-360.
8. Brownlow S., Morais Cabral J. H., Cooper R., Flower D. R., Yewdall S. J., Polikarpov I., North A. C. T., Sawyer L. Bovine β-lactoglobulin at 1.8 Å resolution - still an enigmatic lipocalin. Structure. 5:1997;481-495.
9. Chamberlain A. K., Marqusee S. Molten globule unfolding monitored by hydrogen exchange in urea. Biochemistry. 37:1998;1736-1742.
10. Civera C., Sevilla P., Moreno F., Churchich J. E. Structural changes of β-lactoglobulin B induced by urea. Evidences of residual structure. Biochem. Mol. Biol. Int. 38:1996;773-781.
11. Clarke J., Fersht A. R. An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway. Fold. Design. 1:1996;243-254.
12. Delepierre M., Dobson C. M., Selevarajah S., Wedin R. E., Poulsen F. M. Correlation of hydrogen exchange behaviour and thermal stability of lysozyme. J. Mol. Biol. 168:1983;687-692.
13. Florenzano F. H., Politi M. J. Effect of urea on biomimetic aggregates. Braz. J. Med. Biol. Res. 30:1997;179-185.
14. Fogolari F., Ragona L., Zetta L., Romagnoli S., de Kruif K. G., Molinari H. Monomeric bovine β-lactoglobulin adopts a β-barrel fold at pH 2. FEBS Letters. 436:1998;149-154.
15. 562examined by hydrogen exchange. Biochemistry. 37:1998;3687-3698.
16. Griko Y. V., Kutyshenko V. P. Differences in the processes of β-lactoglobulin cold and heat denaturations. Biophys. J. 67:1994;356-363.
17. Griko Y. V., Privalov P. L. Calorimetric study of the heat and cold denaturation of β-lactoglobulin. Biochemistry. 31:1992;8810-8815.
18. Hamada D., Goto Y. The equilibrium intermediate of β-lactoglobulin with non native α-helical structure. J. Mol. Biol. 269:1997;479-487.
19. Kuwata K., Hoshino M., Era S., Batt C. A., Goto Y. α→β Transition of β-lactoglobulin as evidenced by heteronuclear NMR. J. Mol. Biol. 283:1998;731-739.
20. Lapanje S., Poklar N. Calorimetric and circular dichroic studies of the thermal denaturation of β-lactoglobulin. Biophys. Chem. 34:1989;155-162.
21. Loh S. N., Prehoda K. E., Wang J., Markley J. L. Hydrogen exchange in unligated and ligated staphylococcal nuclease. Biochemistry. 32:1993;11022-11028.
22. Mayo S. L., Baldwin R. L. Guanidinium chloride induction of partial unfolding in amide proton exchange in RNase A. Science. 262:1993;873-876.
23. Molinari H., Ragona L., Varani L., Musco G., Consonni R., Zetta L., Monaco H. L. Partially folded structure of monomeric bovine β-lactoglobulin. FEBS Letters. 381:1996;237-243.
24. Myers J. K., Pace C. N., Scholtz J. M. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4:1995;2138-2148.
25. Pace C. N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131:1986;266-280.
26. Poklar N., Vesnaver G., Lapanje S. Studies by UV spectroscopy of thermal denaturation of β-lactoglobulin in urea and alkylurea solutions. Biophys. Chem. 47:1993;143-151.
27. Qian H., Chan I. S. Hydrogen exchange kinetics of proteins in denaturants: a generalized two-process model. J. Mol. Biol. 286:1999;607-616.
28. Qin B. Y., Bewley M. C., Creamer L. K., Baker M. H., Baker N. E., Jameson G. B. Structural basis of the Tanford transition of bovine β-lactoglobulin. Biochemistry. 37:1998;14014-14023.
29. Qin B. Y., Bewley M. C., Creamer L. K., Baker N. E., Jameson G. B. Functional implications of structural differences between variants A and B of bovine β-lactoglobulin. Protein Sci. 8:1999;75-83.
30. Ragona L., Pusterla F., Zetta L., Monaco H. L., Molinari H. Identification of a conserved hydrophobic cluster in partially folded bovine β-lactoglobulin at pH 2. Fold. Design. 2:1997;281-290.
31. Ragona L., Confalonieri L., Zetta L., de Kruif K. G., Mammi S., Peggion E., Longhi R., Molinari H. Equilibrium unfolding CD studies of bovine β-lactoglobulin and its 14-52 fragment at acidic pH. Biopolymers. 49:1999;441-450.
32. 15N HSQC experiments optimized to retain full sensitivity. J. Magn. Reson. ser. A. 102:1993;241-245.
33. 15N chemical shifts for bovine β-Lactoglobulin: secondary structure and topology of the native state in a partially unfolded form. J. Biomol. NMR. 12:1998;89-107.
34. 2O. FEBS Letters. 421:1998;273-276.
35. Vriend G. WHAT IF: a molecular modelling and drug design program. J. Mol. Graph. 8:1990;52-56.
36. Wagner G., Wüthrich K. Amide proton exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. J. Mol. Biol. 160:1982;343-361.