@article {Craik:2005:0929-8665:147,
title = "Oxidative Folding of the Cystine Knot Motif in Cyclotide Proteins",
journal = "Protein and Peptide Letters",
parent_itemid = "infobike://ben/ppl",
publishercode ="ben",
year = "2005",
volume = "12",
number = "2",
publication date ="2005-02-01T00:00:00",
pages = "147-152",
itemtype = "ARTICLE",
issn = "0929-8665",
url = "https://www.ingentaconnect.com/content/ben/ppl/2005/00000012/00000002/art00006",
doi = "doi:10.2174/0929866053005863",
keyword = "cyclic peptides, circular proteins, conformational folding, kalata b1, nmr",
author = "Craik, David J. and Daly, Norelle L.",
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.",
}