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Article

The folding mechanism of a beta-sheet: the WW domain.

Journal of molecular biology - 10 Aug 2001

Jäger M, Nguyen H, Crane J C, Kelly J W, Gruebele M

Abstract excerpt

The folding thermodynamics and kinetics of the Pin WW domain, a three-stranded antiparallel beta-sheet, have been characterized extensively. Folding and activation free energies were determined as a function of temperature for 16 mutants, which sample all strands and turns of the molecule. The mutational phi value (Phi(m)) diagram is a smooth function of sequence, indicating a prevalence of local interactions in...

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Identifiers

PMID: 11478867
DOI: 10.1006/jmbi.2001.4873

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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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A cross‐strand Trp–Trp pair stabilizes the hPin1 WW domain at the expense of functionSemantic proximity Read ↗

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