Rapid coupling of Surface Plasmon Resonance (SPR and SPRi) and ProteinChip based mass spectrometry for the identification of proteins in nucleoprotein interactions.
We compared coupling approaches of SPR to LC-MS and ProteinChip-based mass spectrometry (SELDI) as a means of identifying proteins captured on DNA surfaces. The approach we outline has the potential to allow multiple, quantitative analysis of macromolecular interactions followed by rapid mass spectrometry identification of retained material.
Bouffartigues
Emeline
E
Enzymologie et cinétique structurale, Laboratoire de Biotechnologies et de Pharmacologie génétique Appliquée, UMR 8113 CNRS, Institut d'Alembert, Ecole Normale Supérieur de Cachan, Cachan, France.
Leh
Hervé
H
Anger-Leroy
Marielle
M
Rimsky
Sylvie
S
Buckle
Malcolm
M
D001426:Bacterial Proteins / Q000032:analysis; D002853:Chromatography, Liquid; D004268:DNA-Binding Proteins / Q000032:analysis*; D009687:Nuclear Proteins / Q000032:analysis*; D040081:Protein Array Analysis; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*; D020349:Surface Plasmon Resonance / Q000379:methods*
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; C031908:H-NS protein, bacteria; D009687:Nuclear Proteins