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Article

Non-standard insulin design: structure-activity relationships at the periphery of the insulin receptor.

Journal of molecular biology - 11 Jan 2002

Weiss Michael A, Wan Zhuli, Zhao Ming, Chu Ying-Chi, Nakagawa Satoe H, Burke G Thomson, Jia Wenhua, Hellmich Rosanna, Katsoyannis Panayotis G

Abstract excerpt

The design of insulin analogues has emphasized stabilization or destabilization of structural elements according to established principles of protein folding. To this end, solvent-exposed side-chains extrinsic to the receptor-binding surface provide convenient sites of modification. An example is provided by an unfavorable helical C-cap (Thr(A8)) whose substitution by favorable amino acids (His(A8) or Arg(A8))...

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Identifiers

PMID: 11779231
DOI: 10.1006/jmbi.2001.5224

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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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