title: Site-selective modification of proteins for the synthesis of structurally defined multivalent scaffolds.
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.
authors: Freie Universität Berlin, Institut für Chemie und Biochemie, Takustr. 3, 14195 Berlin, Germany.
authors: Lukas M
authors: LM
authors: Artner
authors: Lars
authors: L
authors: Merkel
authors: Nina
authors: N
authors: Bohlke
authors: Figen
authors: F
authors: Beceren-Braun
authors: Christoph
authors: C
authors: Weise
authors: Jens
authors: J
authors: Dernedde
authors: Nediljko
authors: N
authors: Budisa
authors: Christian P R
authors: CP
authors: Hackenberger
mesh_terms: D001407:Bacillus / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D001665:Binding Sites; D002241:Carbohydrates / Q000737:chemistry*; D008024:Ligands; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed / Q000379:methods; D011485:Protein Binding; D015202:Protein Engineering / Q000379:methods*
chemical_list: D001426:Bacterial Proteins; D002241:Carbohydrates; D008024:Ligands; C057438:barstar protein, Bacillus amyloliquefaciens