Abstract
A combination of classical site-directed mutagenesis, genetic code engineering and bioorthogonal reactions delivered a chemically modified barstar protein with one or four carbohydrates installed at specific residues. These protein conjugates were employed in multivalent binding studies, which support the use of proteins as structurally defined scaffolds for the presentation of multivalent ligands.
This journal is © The Royal Society of Chemistry 2012
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacillus / chemistry*
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Bacillus / genetics*
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Bacillus / metabolism
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics*
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Bacterial Proteins / metabolism
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Binding Sites
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Carbohydrates / chemistry*
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Ligands
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Models, Molecular
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Mutagenesis, Site-Directed / methods
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Protein Binding
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Protein Engineering / methods*
Substances
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Bacterial Proteins
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Carbohydrates
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Ligands
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barstar protein, Bacillus amyloliquefaciens