| Literature DB >> 21691623 |
Conor M Haney1, Matthew T Loch, W Seth Horne.
Abstract
Covalent side-chain cross-linking has been shown to be a viable strategy to control peptide folding. We report here that an oxime side-chain linkage can elicit α-helical folds from peptides in aqueous solution. The bio-orthogonal bridge is formed rapidly under neutral buffered conditions, and the resulting cyclic oximes are capable of dynamic covalent exchange.Entities:
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Year: 2011 PMID: 21691623 DOI: 10.1039/c1cc12010g
Source DB: PubMed Journal: Chem Commun (Camb) ISSN: 1359-7345 Impact factor: 6.222