Biomolecular Interaction Analysis Coupled With Mass Spectrometry to Detect Interacting Proteins
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With the completion of the human genome sequencing, the objectives of life science have shifted to understanding the functions of proteins. One of the experimental pro- cesses of functional proteomics is the analysis of protein interaction. Surface plasmon resonance (SPR) sensors have become popular technology for the interaction analysis of proteins. The sensors can monitor protein interactions in real-time without labeling molecules. An SPR sensor is unique that it can provide kinetic information on interac- tions, such as association and dissociation rate constants, which often provide clues to evaluate the molecular interaction in terms of protein functions and biological mecha- nisms (1,2). With these features, SPR sensors have been intensively used for “ligand fishing” experiments to identify the binding partner proteins to a specific bait protein (3, 4, 5, 6, 7, 8). Although a binding partner is found in a biological mixture, the task of identify- ing the ligand remains daunting. Purification of the binding partners can be time con- suming and labor intensive, often requiring case-by-case strategies.
KeywordsSurface Plasmon Resonance Tyrosine Hydroxylase Flow Cell Surface Plasmon Resonance Sensor Dissociation Rate Constant
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