Oxidative Folding of the Cystine Knot Motif in Cyclotide Proteins

David   J.   Craik; Norelle   L.   Daly

Abstract

The cyclotides are a large family of plant proteins that have a cyclic backbone and a knotted arrangement of three conserved disulfide bonds. Despite the apparent complexity of their cystine knot motif it is possible to efficiently fold these proteins, as exemplified by oxidative folding studies on the prototypic cyclotide, kalata B1. This mini-review reports on the current understanding of the folding process in cyclotides. The synthesis and folding of these molecules paves the way for their application as stable molecular templates.

Keywords: circular proteins, cyclic peptides, kalata b1, nmr, conformational folding

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Protein & Peptide Letters

Title: Oxidative Folding of the Cystine Knot Motif in Cyclotide Proteins

Volume: 12 Issue: 2

Author(s): David J. Craik and Norelle L. Daly

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Keywords: circular proteins, cyclic peptides, kalata b1, nmr, conformational folding

Abstract: The cyclotides are a large family of plant proteins that have a cyclic backbone and a knotted arrangement of three conserved disulfide bonds. Despite the apparent complexity of their cystine knot motif it is possible to efficiently fold these proteins, as exemplified by oxidative folding studies on the prototypic cyclotide, kalata B1. This mini-review reports on the current understanding of the folding process in cyclotides. The synthesis and folding of these molecules paves the way for their application as stable molecular templates.

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Craik J. David and Daly L. Norelle, Oxidative Folding of the Cystine Knot Motif in Cyclotide Proteins, Protein & Peptide Letters 2005; 12 (2) . https://dx.doi.org/10.2174/0929866053005863