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A peptide model of a protein folding intermediate.

Publication ,  Journal Article
Oas, TG; Kim, PS
Published in: Nature
November 3, 1988

It is difficult to determine the structures of protein folding intermediates because folding is a highly cooperative process. A disulphide-bonded peptide pair, designed to mimic the first crucial intermediate in the folding of bovine pancreatic trypsin inhibitor, contains secondary and tertiary structure similar to that found in the native protein. Peptide models like this circumvent the problem of cooperativity and permit characterization of structures of folding intermediates.

Duke Scholars

Published In

Nature

DOI

ISSN

0028-0836

Publication Date

November 3, 1988

Volume

336

Issue

6194

Start / End Page

42 / 48

Location

England

Related Subject Headings

  • Trypsin Inhibitors
  • Spectrum Analysis
  • Protein Conformation
  • Models, Molecular
  • General Science & Technology
 

Citation

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MLA
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Oas, T. G., & Kim, P. S. (1988). A peptide model of a protein folding intermediate. Nature, 336(6194), 42–48. https://doi.org/10.1038/336042a0
Oas, T. G., and P. S. Kim. “A peptide model of a protein folding intermediate.Nature 336, no. 6194 (November 3, 1988): 42–48. https://doi.org/10.1038/336042a0.
Oas TG, Kim PS. A peptide model of a protein folding intermediate. Nature. 1988 Nov 3;336(6194):42–8.
Oas, T. G., and P. S. Kim. “A peptide model of a protein folding intermediate.Nature, vol. 336, no. 6194, Nov. 1988, pp. 42–48. Pubmed, doi:10.1038/336042a0.
Oas TG, Kim PS. A peptide model of a protein folding intermediate. Nature. 1988 Nov 3;336(6194):42–48.
Journal cover image

Published In

Nature

DOI

ISSN

0028-0836

Publication Date

November 3, 1988

Volume

336

Issue

6194

Start / End Page

42 / 48

Location

England

Related Subject Headings

  • Trypsin Inhibitors
  • Spectrum Analysis
  • Protein Conformation
  • Models, Molecular
  • General Science & Technology