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Article

Stabilization of native protein fold by intein-mediated covalent cyclization.

Journal of molecular biology - 4 Mar 2005

Williams Neal K, Liepinsh Edvards, Watt Stephen J, Prosselkov Pavel, Matthews Jacqueline M, Attard Phil, Beck Jennifer L, Dixon Nicholas E, Otting Gottfried

Abstract excerpt

A mutant version of the N-terminal domain of Escherichia coli DnaB helicase was used as a model system to assess the stabilization against unfolding gained by covalent cyclization. Cyclization was achieved in vivo by formation of an amide bond between the N and C termini with the help of a split mini-intein. Linear and circular proteins were constructed to be identical in amino acid sequence. Mutagenesis of...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 15701520
DOI: 10.1016/j.jmb.2004.12.037

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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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