Quenched Fluorophores Conjugated to Peptides Via Linkers Containing Dithio Groupsġ. NOVEL SOYBEAN PROTEIN MATERIAL AND METHOD FOR PRODUCING THE SAMEĪNTI-FOLATE RECEPTOR ALPHA ANTIBODY GLYCOFORMSīISPECIFIC T CELL ACTIVATING ANTIGEN BINDING MOLECULES Secreted and transmembrane polypeptides and nucleic acids encoding Method for Manufacturing Cubic Diamond Nanocrystalsĭetection of mutations in a gene associated with resistance to viral infection, OAS2 and OAS3 The bispecific constructs were all able to bind both target proteins simultaneously.ĭepartment of Biochemistry, University of Zürich, Winterthurerstrasse 190, CH-8057, Zürich, Switzerland.COMPOSITIONS AND METHODS OF USING CRMP-1 AND ITS FRAGMENTS FOR TREATING CANCERĪTP-binding cassette transporter-like molecules and uses thereof Nine connector modules with distinct geometries were designed for eight of these we were able to confirm the structure by X-ray crystallography, while only one did not crystallize. This allows us to join two or more DARPins in predefined geometries without compromising their binding affinities and specificities. C- and N-terminal DARPin capping repeats were re-designed to be joined by a shared helix in such a way that rigid connector modules are formed. Their ease of in vitro selection, high production yield and stability make them ideal specificity-conferring building blocks for the design of more complex constructs. We use DARPins (Designed Ankyrin Repeat Proteins), synthetic binding proteins based on the Ankyrin-repeat protein scaffold, as binding units. In this study, we demonstrate a method to build up rigid multivalent and multispecific scaffolds by exploiting the modular nature of a repeat protein scaffold and avoiding flexible linkers. Multivalent binding proteins can gain biological activities beyond what is inherent in the individual binders, by bringing together different target molecules, restricting their conformational flexibility or changing their subcellular localization. Funding Organization(s): Swiss National Science Foundation, European Research Council. Deposition Author(s): Batyuk, A., Wu, Y., Mittl, P.R., Plueckthun, A.Expression System: Escherichia coli K-12.Organism(s): synthetic construct, Escherichia coli K-12, Aequorea victoria.5LEL Crystal structure of DARPin-DARPin rigid fusion, variant DD_Off7_10_3G124 in complex with Maltose-binding Protein and Green Fluorescent Protein
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