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Stabilization of native protein fold by intein-mediated covalent cyclization

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


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 Phe102 to Glu rendered the protein monomeric even at high concentration. A difference in...[Show more]

CollectionsANU Research Publications
Date published: 2005
Type: Journal article
Source: Journal of Molecular Biology
DOI: 10.1016/j.jmb.2004.12.037


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