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

doi:10.1016/j.jmb.2004.12.037

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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...

Topics

Adenosine Triphosphatases
Amides
Amino Acid Sequence
Circular Dichroism
Cyclization
DNA Helicases
DnaB Helicases
Entropy
Escherichia coli
Inteins
Kinetics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Magnetic Resonance Spectroscopy

Models, Molecular

Molecular Sequence Data

Mutation

Protein Denaturation

Protein Folding

Protein Structure, Tertiary

Source

Open in PubMed

Identifiers

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

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