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Article

Evidence for subdomain flexibility in Drosophila melanogaster acetylcholinesterase.

Biochemistry - 20 May 2008

Stojan Jure, Ladurantie Caroline, Siadat Omid Ranei, Paquereau Laurent, Fournier Didier

Abstract excerpt

The catalytic domain of the acetylcholinesterases is composed of a single polypeptide chain, the folding of which determines two subdomains. We have linked these two subdomains by mutating two residues, I327 and D375, to cysteines, to form a disulfide bridge. As a consequence, the hydrodynamic radius of the protein was reduced, suggesting that there is some flexibility in the subdomain connection. In addition to...

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Identifiers

PMID: 18439026
DOI: 10.1021/bi7025479

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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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