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Article

Crystal structure of a pH-stabilized mutant of villin headpiece.

Biochemistry - 22 Apr 2008

Meng Jianmin, McKnight C James

Abstract excerpt

Villin-type headpiece domains are compact F-actin-binding motifs that have been used extensively as a model system to investigate protein folding by both experimental and computational methods. Villin headpiece (HP67) harbors a highly helical, thermostable, and autonomously folding subdomain in the C terminus (HP35), and because of this feature, HP67 is usually considered to be composed of a N- and C-terminal...

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PMID: 18370407
DOI: 10.1021/bi7022738

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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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Crystal structure of a pH-stabilized mutant of villin headpiece.PMID 18370407Read ↗

High-resolution crystal structures of villin headpiece and mutants with reduced F-actin binding activity.Semantic proximity Read ↗

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Identification of the PXW sequence as a structural gatekeeper of the headpiece C-terminal subdomain fold.Semantic proximity Read ↗

High-resolution x-ray crystal structures of the villin headpiece subdomain, an ultrafast folding protein.Semantic proximity Read ↗

The fast-folding HP35 double mutant has a substantially reduced primary folding free energy barrier.Semantic proximity Read ↗

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Stabilizing and destabilizing effects of phenylalanine --> F5-phenylalanine mutations on the folding of a small protein.Semantic proximity Read ↗

Common structural transitions in explicit-solvent simulations of villin headpiece folding.Semantic proximity Read ↗

The protein folding network indicates that the ultrafast folding mutant of villin headpiece subdomain has a deeper folding funnel.Semantic proximity Read ↗

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Surface electrostatic networks control hydrophobic core remodeling in a pH-dependent switching proteinSemantic proximity Read ↗

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