title: Surface plasmon resonance based methods for measuring the kinetics and binding affinities of biomolecular interactions.
abstract: Surface plasmon resonance is emerging as the method of choice to study biomolecular interactions between macromolecules because it allows the observation of real-time kinetics for these processes. The method is currently being applied to the study of antigen-antibody interactions, protein-DNA interactions, receptor SH2 domain-phosphotyrosine peptide interactions and receptor-ligand interactions.
authors.affiliation: Laboratory of Cellular Biochemistry, PRI/DynCorp, NCI-Frederick Cancer Research and Development Center, Maryland 21702-1201.
authors.forename: R J
authors.initials: RJ
authors.lastname: Fisher
authors.forename: M
authors.initials: M
authors.lastname: Fivash
mesh_terms: D000937:Antigen-Antibody Reactions; D015374:Biosensing Techniques; D004268:DNA-Binding Proteins / Q000378:metabolism; D007700:Kinetics; D008024:Ligands; D008956:Models, Chemical; D009696:Nucleic Acids / Q000378:metabolism*; D011485:Protein Binding; D011506:Proteins / Q000378:metabolism*; D018160:Receptors, Cytoplasmic and Nuclear / Q000378:metabolism
chemical_list: D004268:DNA-Binding Proteins; D008024:Ligands; D009696:Nucleic Acids; D011506:Proteins; D018160:Receptors, Cytoplasmic and Nuclear