Angewandte Chemie International Edition · 2011 · 95 citations · 23 references
Life SciencesBiochemistryMolecular BiologyProtein EngineeringProtein FoldingStructural BiologyChaperone-assisted FoldingChaperone-mediated FoldingDisulfide Bond FormationMolecular ChaperonesProtein Folding PathwaysProtein MisfoldingDisulfide Bond ChemistryDisulfide Bond MispairingDisulfide ChemistryDisulfide ContributionsDisulfide-bonded IntermediatesNatural Product Total SynthesisProtein Disulfide Bond EngineeringTotal Synthesis-derived Analogues
Secs for your folding problems: Selenocysteine (Sec) residues were used to drive the folding of conotoxin MrVIB, a previously “unfoldable” miniprotein with therapeutic potential (see picture). This simple strategy should generally facilitate the folding of peptides and proteins with multiple disulfide bonds. Detailed facts of importance to specialist readers are published as ”Supporting Information”. Such documents are peer-reviewed, but not copy-edited or typeset. They are made available as submitted by the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
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