Surface plasmon resonance mass spectrometry: recent progress and outlooks.
The combination of surface plasmon resonance (SPR) and mass spectrometry (MS) has created a unique approach to protein investigations. Surface plasmon resonance is used to quantify interactions between proteins and surface-immobilized ligands, and MS is used to determine the structural features of the bound proteins. Recent progress in SPR-MS includes improved methods and operations, increased limits of detection, multi-protein analysis and protein-complex delineation. With the subsequent design of SPR protein arrays, SPR-MS is expected to enter into the field of high-throughput protein interaction discovery and miniaturized diagnostics.
Nedelkov
Dobrin
D
Intrinsic Bioprobes, 625 South Smith Rd, Suite 22, Tempe, AZ 85281, USA. dnedelkov@intrinsicbio.com
Nelson
Randall W
RW
D013058:Mass Spectrometry / Q000295:instrumentation / Q000379:methods* / Q000639:trends*; D008832:Microchemistry / Q000295:instrumentation / Q000379:methods / Q000639:trends; D008970:Molecular Weight; D036103:Nanotechnology / Q000295:instrumentation / Q000379:methods / Q000639:trends; D040081:Protein Array Analysis / Q000295:instrumentation / Q000379:methods* / Q000639:trends*; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000145:classification; D020349:Surface Plasmon Resonance / Q000295:instrumentation / Q000379:methods* / Q000639:trends*; D018511:Systems Integration
D011506:Proteins