Surface plasmon resonance mass spectrometry for protein analysis.
The combination of surface plasmon pesonance (SPR) and mass spectrometry (MS) provides a unique methodology for studying proteins and their interactions. SPR is utilized to assess protein quantitative variations and the kinetic aspects of protein interactions, whereas MS complements the analysis by providing an exclusive look at the structural features of the interacting proteins via measurement of their mass. Thus, intrinsic protein structural modifications that go unregistered via the SPR detection can readily be assessed from the MS data. The purpose of this chapter is dissemination of the procedures and protocols for successful SPR-MS analysis. The individual steps of the complete SPRMS process are illustrated via analysis of cardiac troponin I (cTnI).
Nedelkov
Dobrin
D
Intrinsic Bioprobes Inc., Tempe, AZ, USA.
Nelson
Randall W
RW
D015374:Biosensing Techniques; D001798:Blood Proteins / Q000737:chemistry; D006801:Humans; D008024:Ligands; D013058:Mass Spectrometry / Q000379:methods*; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry*; D040901:Proteomics / Q000379:methods; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000295:instrumentation / Q000379:methods*; D020349:Surface Plasmon Resonance / Q000295:instrumentation / Q000379:methods*; D013997:Time Factors; D019209:Troponin C / Q000737:chemistry
D001798:Blood Proteins; D008024:Ligands; D011506:Proteins; D019209:Troponin C