An examination of the involvement of proline peptide isomerization in protein folding

dc.creatorBabul Cattán, Jorge
dc.creatorNakagawa, Allen
dc.creatorStellwagen, Earle
dc.date.accessioned2018-12-20T14:08:11Z
dc.date.available2018-12-20T14:08:11Z
dc.date.created2018-12-20T14:08:11Z
dc.date.issued1978
dc.identifierJournal of Molecular Biology, Volumen 126, Issue 1, 2018, Pages 117-121
dc.identifier00222836
dc.identifier10.1016/0022-2836(78)90284-X
dc.identifierhttps://repositorio.uchile.cl/handle/2250/154129
dc.description.abstractThe proline peptide isomerization model of protein folding predicts that the fraction of denatured polypeptide chains which rapidly fold should be quantitatively related to the numbers of cis and trans proline residues in the folded polypeptide conformation. However, we find that neither the comparative nor the absolute kinetic pattern for folding of the homologous proteins, tuna heart and horse heart ferricytochrome c which differ by one proline residue, is compatible with the quantitative predictions of the proline peptide isomerization model. © 1978.
dc.languageen
dc.rightshttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
dc.sourceJournal of Molecular Biology
dc.subjectVirology
dc.titleAn examination of the involvement of proline peptide isomerization in protein folding
dc.typeArtículo de revista


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