Surface plasmon resonance based methods for measuring the kinetics and binding affinities of biomolecular interactions.
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.
Fisher
R J
RJ
Laboratory of Cellular Biochemistry, PRI/DynCorp, NCI-Frederick Cancer Research and Development Center, Maryland 21702-1201.
Fivash
M
M
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
D004268:DNA-Binding Proteins; D008024:Ligands; D009696:Nucleic Acids; D011506:Proteins; D018160:Receptors, Cytoplasmic and Nuclear