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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Arsenicals / chemistry*
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Binding Sites
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Cysteine / chemistry*
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Fluorescent Dyes / chemistry
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Green Fluorescent Proteins / chemistry
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Oxazines / chemistry*
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Protein Binding
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Protein Folding
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Protein Structure, Tertiary
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Tumor Suppressor Protein p53 / chemistry
Substances
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Arsenicals
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Fluorescent Dyes
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Oxazines
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ReAsH-EDT2 compound
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Tumor Suppressor Protein p53
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Green Fluorescent Proteins
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Cysteine