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Updated: Jun 22, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
Published on: July 14, 2015
Bipartite tetracysteine display requires site flexibility for ReAsH coordination
Jessica L Goodman1, Daniel B Fried, Alanna Schepartz
1Department of Chemistry, Yale University, 275 Prospect Street, New Haven, CT 06511, USA.
Abstract:
Flexibility required: We designed intramolecular bipartite tetracysteine sites in loops of p53 and the beta-sheets of EmGFP. We found that ReAsH binding preferentially favors tetracysteine sites with flexible geometries such as loops; flexibility was assessed by comparing Calpha B-factor values. This information is important for directing successful bipartite tetracysteine site designs.
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