Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1993 Mar 15;90(6):2099–2100. doi: 10.1073/pnas.90.6.2099

From independent modules to molten globules: observations on the nature of protein folding intermediates.

J Skolnick 1, A Kolinski 1, A Godzik 1
PMCID: PMC46030  PMID: 8460114

Full text

PDF
2099

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Baldwin R. L., Roder H. Characterizing protein folding intermediates. Curr Biol. 1991 Aug;1(4):218–220. doi: 10.1016/0960-9822(91)90061-z. [DOI] [PubMed] [Google Scholar]
  2. Baum J., Dobson C. M., Evans P. A., Hanley C. Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig alpha-lactalbumin. Biochemistry. 1989 Jan 10;28(1):7–13. doi: 10.1021/bi00427a002. [DOI] [PubMed] [Google Scholar]
  3. Briggs M. S., Roder H. Early hydrogen-bonding events in the folding reaction of ubiquitin. Proc Natl Acad Sci U S A. 1992 Mar 15;89(6):2017–2021. doi: 10.1073/pnas.89.6.2017. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Edman J. C., Ellis L., Blacher R. W., Roth R. A., Rutter W. J. Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin. Nature. 1985 Sep 19;317(6034):267–270. doi: 10.1038/317267a0. [DOI] [PubMed] [Google Scholar]
  5. Godzik A., Skolnick J., Kolinski A. Simulations of the folding pathway of triose phosphate isomerase-type alpha/beta barrel proteins. Proc Natl Acad Sci U S A. 1992 Apr 1;89(7):2629–2633. doi: 10.1073/pnas.89.7.2629. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Griko Y. V., Privalov P. L., Venyaminov S. Y., Kutyshenko V. P. Thermodynamic study of the apomyoglobin structure. J Mol Biol. 1988 Jul 5;202(1):127–138. doi: 10.1016/0022-2836(88)90525-6. [DOI] [PubMed] [Google Scholar]
  7. Hughson F. M., Wright P. E., Baldwin R. L. Structural characterization of a partly folded apomyoglobin intermediate. Science. 1990 Sep 28;249(4976):1544–1548. doi: 10.1126/science.2218495. [DOI] [PubMed] [Google Scholar]
  8. Hyde C. C., Ahmed S. A., Padlan E. A., Miles E. W., Davies D. R. Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium. J Biol Chem. 1988 Nov 25;263(33):17857–17871. [PubMed] [Google Scholar]
  9. Jeng M. F., Englander S. W., Elöve G. A., Wand A. J., Roder H. Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR. Biochemistry. 1990 Nov 20;29(46):10433–10437. doi: 10.1021/bi00498a001. [DOI] [PubMed] [Google Scholar]
  10. Kim P. S., Baldwin R. L. Intermediates in the folding reactions of small proteins. Annu Rev Biochem. 1990;59:631–660. doi: 10.1146/annurev.bi.59.070190.003215. [DOI] [PubMed] [Google Scholar]
  11. Kim P. S., Baldwin R. L. Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu Rev Biochem. 1982;51:459–489. doi: 10.1146/annurev.bi.51.070182.002331. [DOI] [PubMed] [Google Scholar]
  12. Kuwajima K. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins. 1989;6(2):87–103. doi: 10.1002/prot.340060202. [DOI] [PubMed] [Google Scholar]
  13. Matouschek A., Serrano L., Fersht A. R. The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure. J Mol Biol. 1992 Apr 5;224(3):819–835. doi: 10.1016/0022-2836(92)90564-z. [DOI] [PubMed] [Google Scholar]
  14. Matouschek A., Serrano L., Meiering E. M., Bycroft M., Fersht A. R. The folding of an enzyme. V. H/2H exchange-nuclear magnetic resonance studies on the folding pathway of barnase: complementarity to and agreement with protein engineering studies. J Mol Biol. 1992 Apr 5;224(3):837–845. doi: 10.1016/0022-2836(92)90565-2. [DOI] [PubMed] [Google Scholar]
  15. Morjana N. A., McKeone B. J., Gilbert H. F. Guanidine hydrochloride stabilization of a partially unfolded intermediate during the reversible denaturation of protein disulfide isomerase. Proc Natl Acad Sci U S A. 1993 Mar 15;90(6):2107–2111. doi: 10.1073/pnas.90.6.2107. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Ptitsyn O. B., Pain R. H., Semisotnov G. V., Zerovnik E., Razgulyaev O. I. Evidence for a molten globule state as a general intermediate in protein folding. FEBS Lett. 1990 Mar 12;262(1):20–24. doi: 10.1016/0014-5793(90)80143-7. [DOI] [PubMed] [Google Scholar]
  17. Ptitsyn O. B., Rashin A. A. Samoorganizatsiia molekuly mioglobina. Dokl Akad Nauk SSSR. 1973 Nov 11;213(2):473–475. [PubMed] [Google Scholar]
  18. Udgaonkar J. B., Baldwin R. L. Early folding intermediate of ribonuclease A. Proc Natl Acad Sci U S A. 1990 Nov;87(21):8197–8201. doi: 10.1073/pnas.87.21.8197. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Udgaonkar J. B., Baldwin R. L. NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A. Nature. 1988 Oct 20;335(6192):694–699. doi: 10.1038/335694a0. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES