Low Noise Detection of Biomolecular Interactions with Signal-Locking Surface Plasmon Resonance

2010 ◽  
Vol 82 (14) ◽  
pp. 6025-6031 ◽  
Author(s):  
Layne D. Williams ◽  
Tridib Ghosh ◽  
Carlos H. Mastrangelo
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Low Noise ◽  
Biomolecular Interactions ◽  
Noise Detection

Integrated Electrokinetic Sample Focusing and Surface Plasmon Resonance Imaging System for Measuring Biomolecular Interactions

2009 ◽  
Vol 81 (5) ◽  
pp. 1957-1963 ◽  
Author(s):  
Ganeshram Krishnamoorthy ◽  
Edwin T. Carlen ◽  
Dietrich Kohlheyer ◽  
Richard B. M. Schasfoort ◽  
Albert van den Berg
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Imaging System ◽  
Biomolecular Interactions ◽  
Surface Plasmon Resonance Imaging ◽  
Resonance Imaging

scholarly journals Surface plasmon resonance: a useful technique for cell biologists to characterize biomolecular interactions

2013 ◽  
Vol 24 (7) ◽  
pp. 883-886 ◽  
Author(s):  
Robert V. Stahelin
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Protein Interactions ◽  
Plasmon Resonance ◽  
Dissociation Rate ◽  
Biomolecular Interactions ◽  
Protein Protein Interactions ◽  
Interaction Kinetics ◽  
Lipid Protein Interactions ◽  
Dissociation Rate Constants

Surface plasmon resonance (SPR) is a powerful technique for monitoring the affinity and selectivity of biomolecular interactions. SPR allows for analysis of association and dissociation rate constants and modeling of biomolecular interaction kinetics, as well as for equilibrium binding analysis and ligand specificity studies. SPR has received much use and improved precision in classifying protein–protein interactions, as well as in studying small-molecule ligand binding to receptors; however, lipid–protein interactions have been underserved in this regard. With the field of lipids perhaps the next frontier in cellular research, SPR is a highly advantageous technique for cell biologists, as newly identified proteins that associate with cellular membranes can be screened rapidly and robustly for lipid specificity and membrane affinity. This technical perspective discusses the conditions needed to achieve success with lipid–protein interactions and highlights the unique lipid–protein interaction mechanisms that have been elucidated using SPR. It is intended to provide the reader a framework for quantitative and confident conclusions from SPR analysis of lipid–protein interactions.

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