Rapid Coupling of Surface Plasmon Resonance (SPR and SPRi) and ProteinChip Based Mass Spectrometry for the Identification of Proteins in Nucleoprotein Interactions

The coupling approaches of SPR to LC-MS and ProteinChip based mass spectrometry (SELDI) has been compared as a means of identifying proteins captured on DNA surfaces. The potential to allow multiple, quantitative analysis of macromolecular interactions followed by rapid mass spectrometry identification of retained material has been studied on the bacterial nucleoid protein H-NS. In this application note, differential H-NS binding to immobilized DNA containing high and low affinity sites has been studied by SPRi and then recovered and identified by mass spectrometry.