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

@article{Williams2005StabilizationON,
  title={Stabilization of native protein fold by intein-mediated covalent cyclization.},
  author={Neal K. Williams and Edvards Liepinsh and Stephen J. Watt and Pavel V. Prosselkov and Jacqueline M Matthews and Phil Attard and Jennifer L Beck and Nicholas E Dixon and Gottfried Otting},
  journal={Journal of molecular biology},
  year={2005},
  volume={346 4},
  pages={
          1095-108
        }
}
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… CONTINUE READING
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Effect of backbone cyclization on protein folding stability: chain entropies of both the unfolded and the folded states are restricted

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