Hydrophobic core variant ubiquitin forms a molten globule conformation at acidic pH

Journal of Biochemistry and Molecular Biology

Volumn 37, Issue 6, 2004, Pages 676-683

  Park, Soon Ho ^a  

^a Gangneung Wonju National University   (South Korea)

Author keywords

Folding intermediate; Molten globule; Ubiquitin

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; TRYPTOPHAN; UBIQUITIN; UREA;

ACIDITY; ARTICLE; CONFORMATION; FLUORESCENCE; GENE MUTATION; HYDROPHOBICITY; PH;

EID: 13544271033     PISSN: 12258687     EISSN: None     Source Type: Journal    
DOI: 10.5483/bmbrep.2004.37.6.676     Document Type: Article

References (31)

1. Anfinsen, C. B. (1973) Principles that govern the folding of protein chains. Science 181, 223-229.
2. Arai, M. and Kuwajima, K. (1996) Rapid formation of a molten globule intermediate in refolding of α-lactalbumin. Fold. Des. 1, 275-287.
3. Azzi, A. (1974) The use of fluorescent probes for the study of membranes. Methods Enzymol. 32, 234-246.
4. Briggs, M. S. and Roder, H. (1992) Early hydrogen-bonding events in the folding reaction of ubiquitin. Proc. Natl. Acad. Sci. USA 89, 2017-2021.
5. Cox, J. P. L., Evans, P. A., Packman, L. C., Williams, D. H. and Woolfson, D. N. (1993) Dissecting the structure of a partially folded protein. Circular dichroism and nuclear magnetic resonance studies of peptides from ubiquitin. J. Mol. Biol. 234, 483-492.
6. Dabora, J. M., Pelton, J. G. and Marqusee, S. (1996) Structure of the acid state of Escherichia coli ribonuclease H1. Biochemistry 35, 11951-11958.
7. Dobson, C. M. (2004) Principles of protein folding, misfolding and aggregation. Semin. Cell Dev. Biol. 15, 3-16.
8. Edelhoch, H. (1967) Spectroscopic Determination of Tryptophan and Tyrosine in Proteins. Biochemistry 6, 1948-1954.
9. Fersht, A. R. (1995) Characterizing transition states in protein folding: an essential step in the puzzle. Curr. Opin. Struct. Biol. 5, 79-84.
10. Fink, A. L. (1998) Protein aggregation: folding aggregates, inclusion bodies and amyloid. Fold. Des. 3, R9-23.
11. Fink, A. L., Calciano, L. J., Goto, Y., Kurotsu, T. and Palleros, D. R. (1994) Classification of Acid Denaturation of Proteins: Intermediates and Unfolded States. Biochemistry 33, 12504-12511.
12. Gladwin, S. T. and Evans, P. A. (1996) Structure of very early protein folding intermediates: new insights through a variant of hydrogen exchange labelling. Fold. Des. 1, 407-417.
13. Goto, Y., Calciano, L. J. and Fink, A. L. (1990) Acid-induced folding of proteins. Proc. Natl. Acad. Sci. USA 87, 573-577.
14. Goto, Y. and Fink, A. L. (1989) Conformational states of β-lactamase: molten-globule states at acidic and alkaline pH with high salt. Biochemistry 28, 945-952.
15. Greenfield, N. and Fasman, G. D. (1969) Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8, 4108-4116.
16. Heidary, D. K., Gross, L. A., Roy, M. and Jennings, P. A. (1997) Evidence for an obligatory intermediate in the folding of interleukin-1β. Nat. Struct. Biol. 4, 725-731.
17. Khorasanizadeh, S., Peters, I. D., Butt, T. R. and Roder, H. (1993) Stability and folding of a tryptophan-containing mutant of ubiquitin. Biochemistry 32, 7054-7063.
18. Khorasanizadeh, S., Peters, I. D. and Roder, H. (1996) Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues. Nat. Struct. Biol. 3, 193-205.
19. Kim, P. S. and Baldwin, R. L. (1982) Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu. Rev. Biochem. 51, 459-489.
20. Kim, P. S. and Baldwin, R. L. (1990) Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59, 631-660.
21. Kuwajima, K., Hiraoka, Y., Ikeguchi, M. and Sugai, S. (1985) Comparison of the transient folding intermediates in lysozyme and α-lactalbumin. Biochemistry 24, 874-881.
22. Laub, P. B., Khorasanizadeh, S. and Roder, H. (1995) Localized solution structure refinement of an F45W variant of ubiquitin using stochastic boundary molecular dynamics and NMR distance restraints. Protein Sci. 4, 973-982.
23. Luo, Y., Kay, M. S. and Baldwin, R. L. (1997) Cooperativity of folding of the apomyoglobin pH 4 intermediate studied by glycine and proline mutations. Nat. Struct. Biol. 4, 925-930.
24. Matthews, C. R. (1993) Pathways of protein folding. Annu. Rev. Biochem. 62, 653-683.
25. Mizuguchi, M., Arai, M., Ke, Y., Nitta, K. and Kuwajima, K. (1998) Equilibrium and kinetics of the folding of equine lysozyme studied by circular dichroism spectroscopy. J. Mol. Biol. 283, 265-277.
26. Ptitsyn, O. B. (1995) Molten globule and protein folding. Adv. Protein Chem. 47, 83-229.
27. Raschke, T. M. and Marqusee, S. (1997) The kinetic folding intermediate of ribonuclease H1 resembles the acid molten globule and partially unfolded molecules detected under native conditions. Nat. Struct. Biol. 4, 298-304.
28. Semisotnov, G. V., Rodionova, N. A., Razgulyaev, O. I., Uversky, V. N., Gripas, A. F. and Gilmanshin, R. I. (1991) Study of the molten globule intermediate state in protein folding by a hydrophobic fluorescent probe. Biopolymers 31, 119-128.
29. Stryer, L. (1968) Fluorescence Spectroscopy of Proteins. Science 162, 526-533.
30. Uversky, V. N. (2002) Cracking the folding code. Why do some proteins adopt partially folded conformations, whereas other don't. FEBS Lett. 514, 181-183.
31. Wilkinson, K. D. and Mayer, A. N. (1986) Alcohol-induced conformational changes of ubiquitin. Arch. Biochem. Biophys. 250, 390-399.