The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor.

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dc.creatorvan Mierlo, C P
dc.creatorDarby, N J
dc.creatorCreighton, T E
dc.date1992-08-01
dc.date.accessioned2026-08-03T01:38:31Z
dc.descriptionThe best-characterized protein folding pathway is that of bovine pancreatic trypsin inhibitor, which folds from the reduced form through a series of disulfide bond intermediates. The crucial one-disulfide intermediate of bovine pancreatic trypsin inhibitor with the disulfide bond between Cys-30 and Cys-51 is shown here to have a partially folded conformation in which the major elements of secondary structure interact via a core of apolar side chains, which resembles part of the native conformation. The stability of this structure can account for the predominance of this one-disulfide intermediate during folding. Much of the remaining one-third of the polypeptide chain, in particular the N-terminal 14 residues, is largely disordered; this accounts for the ability of this intermediate to form readily any of the three possible second disulfide bonds involving Cys-5, -14, and -38. The partially folded conformation of this intermediate provides direct evidence for the importance of native-like interactions between elements of secondary structure in directing protein folding, which is assumed in many studies. IMAGES:
dc.identifierhttps://pmc.ncbi.nlm.nih.gov/articles/PMC49586/
dc.identifierhttps://pubmed.ncbi.nlm.nih.gov/1379719/
dc.identifierhttps://doi.org/10.1073/pnas.89.15.6775
dc.identifier.urihttps://repo.dare.co.zw/handle/123456789/157141
dc.languageen
dc.publisherNational Academy of Sciences
dc.sourceProc Natl Acad Sci U S A
dc.subjectResearch Article
dc.titleThe partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor.
dc.typeText

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