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Article

A cavity-forming mutation in insulin induces segmental unfolding of a surrounding alpha-helix.

Protein science : a publication of the Protein Society - 1 Jan 2002

Xu Bin, Hua Qing-Xin, Nakagawa Satoe H, Jia Wenhua, Chu Ying-Chi, Katsoyannis Panayotis G, Weiss Michael A

Abstract excerpt

To investigate the cooperativity of insulin's structure, a cavity-forming substitution was introduced within the hydrophobic core of an engineered monomer. The substitution, Ile(A2)-->Ala in the A1-A8 alpha-helix, does not impair disulfide pairing between chains. In accord with past studies of cavity-forming mutations in globular proteins, a decrement was observed in thermodynamic stability (DeltaDeltaG(u)...

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Identifiers

PMID: 11742127
DOI: 10.1110/ps.32102
PMCID: PMC2368773

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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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