Surface plasmon resonance: towards an understanding of the mechanisms of biological molecular recognition.
With the introduction of new instruments and improved sensor chip chemistries, surface plasmon resonance (SPR) is finding new applications for molecular interaction studies. Easy access to high-quality kinetic and thermodynamic data for macromolecular binding events is providing insights into the fundamental mechanisms of molecular recognition. Progress is being made to allow larger-scale interaction studies. In addition, combining SPR with other analytical methods is enabling SPR-based analysis of interaction proteomics.
McDonnell
J M
JM
The Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. jim@biop.ox.ac.uk
D000818:Animals; D015374:Biosensing Techniques; D002462:Cell Membrane / Q000378:metabolism*; D004815:Epidermal Growth Factor / Q000378:metabolism; D006801:Humans; D007136:Immunoglobulins / Q000378:metabolism; D007700:Kinetics; D008024:Ligands; D011485:Protein Binding; D012015:Reference Standards; D020349:Surface Plasmon Resonance / Q000295:instrumentation / Q000379:methods*
D007136:Immunoglobulins; D008024:Ligands; D004815:Epidermal Growth Factor