Interactions Responsible for Secondary Structure Formation during Folding of Equine β-Lactoglobulin

Journal of Molecular Biology

Volumn 367, Issue 4, 2007, Pages 1205-1214

  Nakagawa, Kanako ^a   Yamada, Yoshiteru ^a   Fujiwara, Kazuo ^a   Ikeguchi, Masamichi ^a  

^a SOKA UNIVERSITY   (Japan)

Author keywords

circular dichroism; hydrophobic interaction; molten globule; peptide; proline mutant

Indexed keywords

ALANINE; BETA LACTOGLOBULIN; CYSTEINE; MUTANT PROTEIN; PEPTIDE FRAGMENT; PROLINE; PROTEIN CHIBL; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; DISULFIDE BOND; HORSE; HYDROPHOBICITY; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; SITE DIRECTED MUTAGENESIS;

EQUIDAE;

EID: 33847702924     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.01.053     Document Type: Article

References (39)

1. Arai M., and Kuwajima K. Role of the molten globule state in protein folding. Advan. Protein Chem. 53 (2000) 209-282
2. Barrick D., and Baldwin R.L. Stein and Moore Award address. The molten globule intermediate of apomyoglobin and the process of protein folding. Protein Sci. 2 (1993) 869-876
3. Waltho J.P., Feher V.A., Merutka G., Dyson H.J., and Wright P.E. Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobin. Biochemistry 32 (1993) 6337-6347
4. Kuroda Y. Residual helical structure in the C-terminal fragment of cytochrome c. Biochemistry 32 (1993) 1219-1224
5. Shimizu A., Ikeguchi M., Kobayashi T., and Sugai S. A synthetic peptide study on the molten globule of α-lactalbumin. J. Biochem. (Tokyo) 119 (1996) 947-952
6. Demarest S.J., Fairman R., and Raleigh D.P. Peptide models of local and long-range interactions in the molten globule state of human α-lactalbumin. J. Mol. Biol. 283 (1998) 279-291
7. Wu L.C., Laub P.B., Elove G.A., Carey J., and Roder H. A noncovalent peptide complex as a model for an early folding intermediate of cytochrome c. Biochemistry 32 (1993) 10271-10276
8. Ikeguchi M., and Sugai S. Contribution of disulfide bonds to stability of the folding intermediate of α-lactalbumin. Int. J. Pept. Protein Res. 33 (1989) 289-297
9. Goto Y., Calciano L.J., and Fink A.L. Acid-induced folding of proteins. Proc. Natl Acad. Sci. USA 87 (1990) 573-577
10. Kataoka M., Hagihara Y., Mihara K., and Goto Y. Molten globule of cytochrome c studied by small angle X-ray scattering. J. Mol. Biol. 229 (1993) 591-596
11. Kataoka M., Nishii I., Fujisawa T., Ueki T., Tokunaga F., and Goto Y. Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering. J. Mol. Biol. 249 (1995) 215-228
12. Kuroda Y., Kidokoro S., and Wada A. Thermodynamic characterization of cytochrome c at low pH. Observation of the molten globule state and of the cold denaturation process. J. Mol. Biol. 223 (1992) 1139-1153
13. Nishii I., Kataoka M., and Goto Y. Thermodynamic stability of the molten globule states of apomyoglobin. J. Mol. Biol. 250 (1995) 223-238
14. Sabelko J., Ervin J., and Gruebele M. Cold-denatured ensemble of apomyoglobin: implications for the early steps of folding. J. Phys. Chem. B 102 (1998) 1806-1819
15. Sawyer L., and Kontopidis G. The core lipocalin, bovine β-lactoglobulin. Biochim. Biophys. Acta 1482 (2000) 136-148
16. Kuwajima K., Yamaya H., Miwa S., Sugai S., and Nagamura T. Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism. FEBS Letters 221 (1987) 115-118
17. Kuwajima K., Yamaya H., and Sugai S. The burst-phase intermediate in the refolding of β-lactoglobulin studied by stopped-flow circular dichroism and absorption spectroscopy. J. Mol. Biol. 264 (1996) 806-822
18. Hamada D., Segawa S., and Goto Y. Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein. Nature Struct. Biol. 3 (1996) 868-873
19. Fujiwara K., Arai M., Shimizu A., Ikeguchi M., Kuwajima K., and Sugai S. Folding-unfolding equilibrium and kinetics of equine β-lactoglobulin: equivalence between the equilibrium molten globule state and a burst-phase folding intermediate. Biochemistry 38 (1999) 4455-4463
20. Ikeguchi M., Kato S., Shimizu A., and Sugai S. Molten globule state of equine β-lactoglobulin. Proteins: Struct. Funct. Genet. 27 (1997) 567-575
21. Yamada Y., Yajima T., Fujiwara K., Arai M., Ito K., Shimizu A., et al. Helical and expanded conformation of equine β-lactoglobulin in the cold-denatured state. J. Mol. Biol. 350 (2005) 338-348
22. Yamada Y., Nakagawa K., Yajima T., Saito K., Tokushima A., Fujiwara K., and Ikeguchi M. Structural and thermodynamic consequences of removal of a conserved disulfide bond from equine β-lactoglobulin. Proteins: Struct. Funct. Bioinf. 63 (2006) 595-602
23. Yamada, Y., Yajima, T., Tsukamoto, S., Nakagawa, K., Fujiwara, K., Kihara, H. & Ikeguchi, M. (2006). Chloride ion concentration dependence of molecular dimension in the acid-denatured state of equine β-lactoglobulin. J. Appl. Crystallor. In the press.
24. Kobayashi T., Ikeguchi M., and Sugai S. Molten globule structure of equine β-lactoglobulin probed by hydrogen exchange. J. Mol. Biol. 299 (2000) 757-770
25. Nakagawa K., Tokushima A., Fujiwara K., and Ikeguchi M. Proline scanning mutagenesis reveals non-native fold in the molten globule state of equine β-lactoglobulin. Biochemistry 45 (2006) 15468-15473
26. Hamada D., Kuroda Y., Tanaka T., and Goto Y. High helical propensity of the peptide fragments derived from β-lactoglobulin, a predominantly β-sheet protein. J. Mol. Biol. 254 (1995) 737-746
27. Ragona L., Catalano M., Zetta L., Longhi R., Fogolari F., and Molinari H. Peptide models of folding initiation sites of bovine β-lactoglobulin: identification of nativelike hydrophobic interactions involving G and H strands. Biochemistry 41 (2002) 2786-2796
28. Ikeguchi M., Fujino M., Kato M., Kuwajima K., and Sugai S. Transition state in the folding of α-lactalbumin probed by the 6-120 disulfide bond. Protein Sci. 7 (1998) 1564-1574
29. Demarest S.J., Boice J.A., Fairman R., and Raleigh D.P. Defining the core structure of the α-lactalbumin molten globule state. J. Mol. Biol. 294 (1999) 213-221
30. Shin H.C., Merutka G., Waltho J.P., Tennant L.L., Dyson H.J., and Wright P.E. Peptide models of protein folding initiation sites. 3. The G-H helical hairpin of myoglobin. Biochemistry 32 (1993) 6356-6364
31. Privalov P.L., and Gill S.J. Stability of protein structure and hydrophobic interaction. Advan. Protein Chem. 39 (1988) 191-234
32. Hughson F.M., Barrick D., and Baldwin R.L. Probing the stability of a partly folded apomyoglobin intermediate by site-directed mutagenesis. Biochemistry 30 (1991) 4113-4118
33. Kay M.S., and Baldwin R.L. Packing interactions in the apomyglobin folding intermediate. Nature Struct. Biol. 3 (1996) 439-445
34. Kay M.S., Ramos C.H., and Baldwin R.L. Specificity of native-like interhelical hydrophobic contacts in the apomyoglobin intermediate. Proc. Natl Acad. Sci. USA 96 (1999) 2007-2012
35. Marmorino J.L., and Pielak G.J. A native tertiary interaction stabilizes the A state of cytochrome c. Biochemistry 34 (1995) 3140-3143
36. Wu L.C., and Kim P.S. Hydrophobic sequence minimization of the α-lactalbumin molten globule. Proc. Natl Acad. Sci. USA 94 (1997) 14314-14319
37. Wu L.C., and Kim P.S. A specific hydrophobic core in the α-lactalbumin molten globule. J. Mol. Biol. 280 (1998) 175-182
38. Gill S.C., and von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182 (1989) 319-326
39. Brownlow S., Morais Cabral J.H., Cooper R., Flower D.R., Yewdall S.J., Polikarpov I., et al. Bovine β-lactoglobulin at 1.8 Å resolution-still an enigmatic lipocalin. Structure 5 (1997) 481-495