Site-selective modification of proteins for the synthesis of structurally defined multivalent scaffoldsThis article is part of the ChemComm Glycochemistry and glycobiology web themed issue.Electronic supplementary information (ESI) available: Brief outline of the synthesis, MALDI-spectra. See DOI: 10.1039/c1cc16039g

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. A combination of genetic code engineering and bioorthogonal functionalization was employed to obtain an artificial protein scaffold for multivalent binding studies with one or four carbohydrates installed at specific residues.