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Article

Changes in secondary structure follow the dissociation of human insulin hexamers: a circular dichroism study.

Proteins - 1 Jan 1990

Melberg S G, Johnson W C

Abstract excerpt

Vacuum UV circular dichroism spectra measured down to 178 nm for hexameric 2-zinc human insulin, zinc-free human insulin, and the two engineered and biologically active monomeric mutants, [B/S9D] and [B/S9D,T27E] human insulin, show significant differences. The secondary structure analysis of the 2-zinc human insulin (T6) in neutral solution was determined: 57% helix, 1% beta-strand, 18% turn, and 24% random...

Topics

Circular Dichroism
Humans
Insulin
Mutation
Protein Conformation
X-Ray Diffraction
Zinc

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 2281088
DOI: 10.1002/prot.340080309

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2281088-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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