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Article

Engineering the independent folding of the subtilisin BPN' prodomain: analysis of two-state folding versus protein stability.

Biochemistry - 26 Aug 1997

Ruvinov S, Wang L, Ruan B, Almog O, Gilliland G L, Eisenstein E, Bryan P N

Abstract excerpt

In complex with subtilisin BPN', the 77 amino acid prodomain folds into a stable compact structure comprising a four-stranded antiparallel beta-sheet and two three-turn alpha-helices. When isolated from subtilisin, the prodomain is 97% unfolded even under optimal folding conditions. Traditionally, to study stable proteins, denaturing cosolvents or temperatures are used to shift the equilibrium from folded to...

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Identifiers

PMID: 9265621
DOI: 10.1021/bi9703958

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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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Engineering the independent folding of the subtilisin BPN' prodomain: analysis of two-state folding versus protein stability.PMID 9265621Read ↗

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