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Article

Atomic force microscopy of crystalline insulins: the influence of sequence variation on crystallization and interfacial structure.

Biophysical journal - 1 May 1998

Yip C M, Brader M L, DeFelippis M R, Ward M D

Abstract excerpt

The self-association of proteins is influenced by amino acid sequence, molecular conformation, and the presence of molecular additives. In the presence of phenolic additives, LysB28ProB29 insulin, in which the C-terminal prolyl and lysyl residues of wild-type human insulin have been inverted, can be crystallized into forms resembling those of wild-type insulins in which the protein exists as zinc-complexed...

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Identifiers

PMID: 9591647
DOI: 10.1016/S0006-3495(98)77929-9
PMCID: PMC1299563

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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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