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Article

Accelerated refolding of subtilisin BPN' by tertiary-structure-forming mutants of its propeptide.

Journal of biochemistry - 1 Oct 2001

Kojima S, Yanai H, Miura K

Abstract excerpt

The propeptide of subtilisin BPN', which functions as an intramolecular chaperone and a temporary inhibitor of subtilisin, is unique in that it acquires its three-dimensional structure by formation of a complex with the cognate protease. We previously showed that the successive amino acid replacements Ala47-->Phe, Gly13-->Ile, and Val65-->Ile in the propeptide to increase its hydrophobicity resulted in formation...

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Source

Identifiers

PMID: 11574065
DOI: 10.1093/oxfordjournals.jbchem.a003008

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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