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Article

Buried hydrophobic side-chains essential for the folding of the parallel beta-helix domains of the P22 tailspike.

Protein science : a publication of the Protein Society - 1 Sept 2004

Betts Scott, Haase-Pettingell Cameron, Cook Kristen, King Jonathan

Abstract excerpt

The processive beta-strands and turns of a polypeptide parallel beta-helix represent one of the topologically simplest beta-sheet folds. The three subunits of the tailspike adhesin of phage P22 each contain 13 rungs of a parallel beta-helix followed by an interdigitated section of triple-stranded beta-helix. Long stacks of hydrophobic residues dominate the elongated buried core of these two beta-helix domains and...

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Source

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Identifiers

PMID: 15322277
DOI: 10.1110/ps.04676704
PMCID: PMC2280027

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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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