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Article

Analysis of core packing in a cooperatively folded miniature protein: the ultrafast folding villin headpiece helical subdomain.

Biochemistry - 2 Jun 2009

Xiao Shifeng, Bi Yuan, Shan Bing, Raleigh Daniel P

Abstract excerpt

The helical subdomain of the villin headpiece is the smallest naturally occurring cooperatively folded protein. Its small size, simple three-helix topology, and very rapid folding have made it an extremely popular model system for computational and theoretical studies of protein folding. The domain has a well-packed hydrophobic core comprised in part of an unusual set of three closely packed phenylalanine...

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Identifiers

PMID: 19354264
DOI: 10.1021/bi8021763

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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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Analysis of core packing in a cooperatively folded miniature protein: the ultrafast folding villin headpiece helical subdomain.PMID 19354264Read ↗

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

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

Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing.Semantic proximity Read ↗

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

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Robust folding of a de novo designed ideal protein even with most of the core mutated to valine.Semantic proximity Read ↗

Ultrafast folding kinetics and cooperativity of villin headpiece in single-molecule force spectroscopy.Semantic proximity Read ↗

Quantitative comparison of villin headpiece subdomain simulations and triplet-triplet energy transfer experiments.Semantic proximity Read ↗

The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology.Semantic proximity Read ↗

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