Proteins can adopt totally different folded conformations

Journal of Molecular Biology

Volumn 291, Issue 3, 1999, Pages 715-725

  Damaschun, Gregor ^a   Damaschun, Hilde ^b   Gast, Klaus ^b   Zirwer, Dietrich ^b  

^a HUMBOLDT UNIVERSITY   (Germany)

^b MAX DELBRÜCK CENTER FOR MOLECULAR MEDICINE   (Germany)

Author keywords

Misfolding; Non native structures; Polymorphism; Protein denaturation; Protein folding

Indexed keywords

ACID; AMYLOID; ANION; CHLORIDE; PHOSPHOGLYCERATE KINASE; TRICHLOROACETIC ACID;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; IONIC STRENGTH; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; YEAST;

EID: 0033588342     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3009     Document Type: Article

References (39)

1. Adams B., Burgess R. J., Pain R. H. The folding and mutual interaction of the domains of yeast 3-phosphoglycerate kinase. Eur. J. Biochem. 152:1985;715-720.
2. Anfinsen C. B. Principles that govern the folding of protein chains. Science. 181:1973;223-230.
3. Benoit H., Doty P. Light scattering from non-Gaussian chains. J. Phys. Chem. 57:1953;958-963.
4. Chiti F., Webster P., Taddei N., Clark A., Stefani M., Ramponi G., Dobson C. M. Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc. Natl Acad. Sci. USA. 96:1999;3590-3594.
5. Damaschun G., Damaschun H., Gast K., Misselwitz R., Müller J. J., Pfeil W., Zirwer D. Cold denaturation-induced conformational changes in phosphoglycerate kinase from yeast. Biochemistry. 32:1993;7739-7746.
6. Damaschun G., Damaschun H., Gast K., Zirwer D. Denatured states of yeast phosphoglycerate kinase. Biochemistry (Moscow). 63:1998;259-275.
7. 1with intact disulfide bonds: a study by small-angle X-ray scattering. Biochim. Biophys. Acta. 1340:1997;235-244.
8. Dandekar T., König R. Computational methods for the prediction of protein folds. Biochim. Biophys. Acta. 1343:1997;1-15.
9. Davies S. M. A., Kelly S. M., Price N. C., Bradshaw J. P. Structural plasticity of the feline leukaemia virus fusion peptide: a circular dichroism study. FEBS Letters. 425:1998;415-418.
10. Dobson C. M., Sali A., Karplus M. Protein folding: a perspective from theory and experiment. Angew. Chem. Int. Ed. 37:1998;868-893.
11. Fink A. L. Compact intermediate states in protein folding. Annu. Rev. Biophys. Biomol. Struct. 24:1995;495-522.
12. Fink A. L., Calciano L. J., Goto Y., Kurotsu T., Palleros D. R. Classification of acid denaturation of proteins: intermediates and unfolded states. Biochemistry. 33:1994;12504-12511.
13. Fink A. L., Oberg K. A., Seshadri S. Discrete intermediates versus molten globule models for protein folding: characterization of partially folded intermediates of apomyoglobin. Fold. Design. 3:1997;19-25.
14. Flory P. J. Statistical Mechanics of Chain Molecules. 1988;Oxford University Press, New York. p. 248-306.
15. Garcia de la Torre J., Bloomfield V. A. Hydrodynamic properties of complex, rigid, biological macromolecules: theory and applications. Quart. Rev. Biophys. 14:1981;81-139.
16. Gast K., Damaschun G., Misselwitz R., Zirwer D. Application of dynamic light scattering to studies of protein folding kinetics. Eur. Biophys. J. 21:1992;357-362.
17. Gast K., Nöppert A., Müller-Frohne M., Zirwer D., Damaschun G. Stopped-flow dynamic light scattering as a method to monitor compaction during protein folding. Eur. Biophys. J. 25:1997;211-219.
18. Goto Y., Takahashi N., Fink A. L. Mechanism of acid-induced folding of proteins. Biochemistry. 29:1990;3480-3488.
19. Harrison P. M., Bamborough P., Daggett V., Prusiner S. B., Cohen F. E. The prion folding problem. Curr. Opin. Struct. Biol. 7:1997;53-59.
20. Hornemann S., Glockshuber R. A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pH. Proc. Natl Acad. Sci. USA. 95:1998;6010-6014.
21. Johnson W. C. Jr. Protein secondary structure and circular dichroism: a practical guide. Proteins: Struct. Funct. Genet. 7:1990;205-214.
22. Kabsch W., Sander C. On the use of sequence homologies to predict protein structure: identical pentapeptides can have different conformations. Proc. Natl Acad. Sci. USA. 81:1984;1075-1078.
23. Kirste R. G., Oberthür R. C. Synthetic polymers in solution. Glatter O., Kratky O. Small-angle X-ray Scattering. 1982;387-431 Academic Press, London.
24. Koppel D. E. Analysis of macromolecular polydispersity in intensity correlation spectroscopy: the method of cumulants. J. Chem. Phys. 57:1972;4814-4820.
25. Lansbury P. T. Jr. Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease. Proc. Natl Acad. Sci. USA. 96:1999;3342-3344.
26. Minor D. L. Jr, Kim P. S. Context dependent secondary structure formation of a designed protein sequence. Nature. 380:1986;730-734.
27. Missiakas D., Betton J. M., Minard P., Yon J. M. Unfolding-refolding of the domains in yeast phosphoglycerate kinase: comparison with the isolated engineered domains. Biochemistry. 29:1990;8683-8868.
28. Provencher S. W. A constrained regularization method for inverting data presented by linear algebraic or integral equations. Comp. Phys. Commun. 27:1982a;213-227.
29. Provencher S. W. A general purpose constrained regularization program for inverting noisy linear algebraic or integral equations. Comp. Phys. Commun. 27:1982b;229-242.
30. Provencher S. W., Glöckner J. Estimation of globular protein secondary structure from circular dichroism. Biochemistry. 20:1981;33-37.
31. Rost B., O'Donoghue S. Sisyphus and prediction of protein structure. CABIOS. 13:1997;345-356.
32. 2synthase amino-terminal domain. Biochemistry. 37:1998;822-830.
33. Sirokman G., Fasman G. D. Refolding and protein pumping activity of a glycol-bacteriorhodopsin water-soluble conjugate. Protein Sci. 2:1993;1161-1170.
34. Sudarsanam S. Structural diversity of sequentially identical subsequences of proteins: identical octapeptides can have different conformations. Proteins: Struct. Funct. Genet. 30:1998;228-231.
35. Sunde M., Blake C. C. F. From the globular to fibrous state: protein structure and structural conversion in amyloid formation. Quart. Rev. Biophys. 31:1998;1-39.
36. Uversky V. N., Karnoup A. S., Segel D. J., Seshadri S., Doniach S., Fink A. L. Anion-induced folding of staphylococcal nuclease: characterization of multiple equilibrium partially folded intermediates. J. Mol. Biol. 278:1998a;879-894.
37. Uversky V. N., Segel D. J., Doniach S., Fink A. L. Association-induced folding of globular proteins. Proc. Natl Acad. Sci. USA. 95:1998b;5480-5483.
38. Walgers R., Lee T. C., Cammers-Goodwin A. An indirect chaotropic mechanism for the stabilization of helix conformation of peptides in aqueous trifluoroethanol and hexafluoro-2-propanol. J. Am. Chem. Soc. 120:1998;5073-5079.
39. Watson H. C., Walker N. P. C., Shaw P. J., Bryant T. N., Wendell P. L., Fothergill L. A., Perkins R. E., Conroy S. C., Dobson M. J., Tuite M. F., Kingsman A. J., Kingsman S. M. Sequence and structure of yeast phosphoglycerate kinase. EMBO J. 1:1982;1635-1640.