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Article

Apparent two-state tendamistat folding is a sequential process along a defined route.

Journal of molecular biology - 16 Feb 2001

Bachmann A, Kiefhaber T

Abstract excerpt

The small all-beta-sheet protein tendamistat folds and unfolds rapidly in apparent two-state reactions. Kinetic measurements of two tendamistat variants under various solvent conditions reveal, however, that folding occurs in at least two sequential steps through a metastable obligatory intermediate. Depending on the solvent conditions either step can become rate limiting. The activation parameters indicate that...

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Identifiers

PMID: 11237606
DOI: 10.1006/jmbi.2000.4399

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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