title: Analysis of protein ligand-receptor binding by photoaffinity cross-linking.
abstract: Photoaffinity cross-linking is a rapidly developing technology for studying biomolecular interactions, including protein ligand-receptor binding. This technology provides detailed binding information including receptor contact sites, active conformation of receptor-ligand complexes, global binding surfaces, and binding modes. Advancements in genetic technology have enabled non-natural photoactive amino acid derivatives to be incorporated into designer or target proteins, providing a host of new opportunities for manufacturing protein photo-probes while bypassing the traditional peptide or small protein limits of classical chemical synthesis. This unit provides several protocols for performing basic photoaffinity cross-linking and related analyses for applications in ligand-receptor binding and protein-protein interactions.
authors: Department of Biochemistry and Center for Drug Discovery, Virginia Polytechnic Institute and State University, Blacksburg, Virginia.
authors: Ling
authors: L
authors: Wu
authors: Department of Biochemistry and Center for Drug Discovery, Virginia Polytechnic Institute and State University, Blacksburg, Virginia.
authors: Bin
authors: B
authors: Xu
mesh_terms: D001665:Binding Sites; D003432:Cross-Linking Reagents / Q000737:chemistry*; D008024:Ligands; D010449:Peptide Mapping / Q000379:methods*; D019920:Photoaffinity Labels / Q000737:chemistry*; D011485:Protein Binding
chemical_list: D003432:Cross-Linking Reagents; D008024:Ligands; D019920:Photoaffinity Labels
keywords: biosynthetic photo-probe; ligand-receptor binding; mapping of binding sites; photoaffinity cross-linking; protein-protein interaction