Skip to main content
PMC 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
. 1996 Apr 2;93(7):2627–2628. doi: 10.1073/pnas.93.7.2627

Why is protein folding so fast?

R L Baldwin 1
PMCID: PMC39680  PMID: 8610091

Full text

PDF
2628

Selected References

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

  1. Burgering M. J., Hald M., Boelens R., Breg J. N., Kaptein R. Hydrogen exchange studies of the Arc repressor: evidence for a monomeric folding intermediate. Biopolymers. 1995 Feb;35(2):217–226. doi: 10.1002/bip.360350210. [DOI] [PubMed] [Google Scholar]
  2. Fersht A. R. Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications. Proc Natl Acad Sci U S A. 1995 Nov 21;92(24):10869–10873. doi: 10.1073/pnas.92.24.10869. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Hammes G. G., Roberts P. B. Dynamics of the helix--coil transition in poly-L-ornithine. J Am Chem Soc. 1969 Mar 26;91(7):1812–1816. doi: 10.1021/ja01035a036. [DOI] [PubMed] [Google Scholar]
  4. Huang G. S., Oas T. G. Submillisecond folding of monomeric lambda repressor. Proc Natl Acad Sci U S A. 1995 Jul 18;92(15):6878–6882. doi: 10.1073/pnas.92.15.6878. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Jackson S. E., Fersht A. R. Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. Biochemistry. 1991 Oct 29;30(43):10428–10435. doi: 10.1021/bi00107a010. [DOI] [PubMed] [Google Scholar]
  6. Karplus M., Weaver D. L. Protein-folding dynamics. Nature. 1976 Apr 1;260(5550):404–406. doi: 10.1038/260404a0. [DOI] [PubMed] [Google Scholar]
  7. Lumry R., Biltonen R. Validity of the "two-state" hypothesis for conformational transitions of proteins. Biopolymers. 1966 Sep;4(8):917–944. doi: 10.1002/bip.1966.360040808. [DOI] [PubMed] [Google Scholar]
  8. Milla M. E., Sauer R. T. P22 Arc repressor: folding kinetics of a single-domain, dimeric protein. Biochemistry. 1994 Feb 8;33(5):1125–1133. doi: 10.1021/bi00171a011. [DOI] [PubMed] [Google Scholar]
  9. Pohl F. M. Einfache Temperatursprung-Methode im Sekunden-bis Stundenbereich und die reversible denaturierung von Chymotrypsin. Eur J Biochem. 1968 Apr;4(3):373–377. doi: 10.1111/j.1432-1033.1968.tb00221.x. [DOI] [PubMed] [Google Scholar]
  10. Pohl F. M. Kinetics of reversible denaturation of trypsin in water and water--ethanol mixtures. Eur J Biochem. 1968 Dec;7(1):146–152. doi: 10.1111/j.1432-1033.1968.tb19585.x. [DOI] [PubMed] [Google Scholar]
  11. Pohl F. M. On the kinetics of structural transition I of some pancreatic proteins. FEBS Lett. 1969 Apr;3(1):60–64. doi: 10.1016/0014-5793(69)80097-9. [DOI] [PubMed] [Google Scholar]
  12. SCHWARZ G. ON THE KINETICS OF THE HELIX-COIL TRANSITION OF POLYPEPTIDES IN SOLUTION. J Mol Biol. 1965 Jan;11:64–77. doi: 10.1016/s0022-2836(65)80171-1. [DOI] [PubMed] [Google Scholar]
  13. Schindler T., Herrler M., Marahiel M. A., Schmid F. X. Extremely rapid protein folding in the absence of intermediates. Nat Struct Biol. 1995 Aug;2(8):663–673. doi: 10.1038/nsb0895-663. [DOI] [PubMed] [Google Scholar]
  14. Waldburger C. D., Jonsson T., Sauer R. T. Barriers to protein folding: formation of buried polar interactions is a slow step in acquisition of structure. Proc Natl Acad Sci U S A. 1996 Apr 2;93(7):2629–2634. doi: 10.1073/pnas.93.7.2629. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Waldburger C. D., Schildbach J. F., Sauer R. T. Are buried salt bridges important for protein stability and conformational specificity? Nat Struct Biol. 1995 Feb;2(2):122–128. doi: 10.1038/nsb0295-122. [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