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Article

Influence of hPin1 WW N-terminal domain boundaries on function, protein stability, and folding.

Protein science : a publication of the Protein Society - 1 Jul 2007

Jäger Marcus, Nguyen Houbi, Dendle Maria, Gruebele Martin, Kelly Jeffery W

Abstract excerpt

An N-terminally truncated and cooperatively folded version (residues 6-39) of the human Pin1 WW domain (hPin1 WW hereafter) has served as an excellent model system for understanding triple-stranded beta-sheet folding energetics. Here we report that the negatively charged N-terminal sequence (Met1-Ala-Asp-Glu-Glu5) previously deleted, and which is not conserved in highly homologous WW domain family members from...

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Identifiers

PMID: 17586778
DOI: 10.1110/ps.072775507
PMCID: PMC2206688

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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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