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
APA
Chicago
ICMJE
MLA
NLM
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.
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