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Article

Circularly permuted variants of the green fluorescent protein.

FEBS letters - 27 Aug 1999

Topell S, Hennecke J, Glockshuber R

Abstract excerpt

Folding of the green fluorescent protein (GFP) from Aequorea victoria is characterized by autocatalytic formation of its p-hydroxybenzylideneimidazolidone chromophore, which is located in the center of an 11-stranded beta-barrel. We have analyzed the in vivo folding of 20 circularly permuted variants of GFP and find a relatively low tolerance towards disruption of the polypeptide chain by introduction of new...

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Identifiers

PMID: 10471794
DOI: 10.1016/s0014-5793(99)01044-3

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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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