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Article

Protein folding: adding a nucleus to guide helix docking reduces landscape roughness.

Journal of molecular biology - 26 Oct 2012

Wensley Beth G, Kwa Lee Gyan, Shammas Sarah L, Rogers Joseph M, Clarke Jane

Abstract excerpt

The elongated three-helix-bundle spectrin domains R16 and R17 fold and unfold unusually slowly over a rough energy landscape, in contrast to the homologue R15, which folds fast over a much smoother, more typical landscape. R15 folds via a nucleation-condensation mechanism that guides the docking of the A and C-helices. However, in R16 and R17, the secondary structure forms first and the two helices must then dock...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 22917971
DOI: 10.1016/j.jmb.2012.08.003
PMCID: PMC3469821

Provenance

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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