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Article

Structural characterization of a trapped folding intermediate of pyrrolidone carboxyl peptidase from a hyperthermophile.

Biochemistry - 7 Aug 2012

Mizuguchi Mineyuki, Takeuchi Makoto, Ohki Shinya, Nabeshima Yuko, Kouno Takahide, Aizawa Tomoyasu, Demura Makoto, Kawano Keiichi, Yutani Katsuhide

Abstract excerpt

The refolding of cysteine-free pyrrolidone carboxyl peptidase (PCP-0SH) from a hyperthermophile is unusually slow. PCP-0SH is trapped in the denatured (D1) state at 4 °C and pH 2.3, which is different from the highly denatured state in the presence of concentrated denaturant. In order to elucidat...

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PMID: 22799522
DOI: 10.1021/bi300608e

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-22799522-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

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