Browsing by Subject "Binding affinity"

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    Using Surface Plasmon Resonance to Quantitatively Assess Lipid-Protein Interactions
    (Springer, 2016) Del Vecchio, Kathryn; Stahelin, Robert V.; Biochemistry and Molecular Biology, School of Medicine
    Surface Plasmon Resonance (SPR) is a quantitative, label-free method for determining molecular interactions in real time. The technology involves fixing a ligand onto a senor chip, measuring a baseline resonance angle, and flowing an analyte in bulk solution over the fixed ligand to measure the subsequent change in resonance angle. The mass of analyte bound to fixed ligand is directly proportional to the resonance angle change and the system is sensitive enough to detect as little as picomolar amounts of analyte in the bulk solution. SPR can be used to determine both the specificity of molecular interactions and the kinetics and affinity of an interaction. This technique has been especially useful in measuring the affinities of lipid-binding proteins to intact liposomes of varying lipid compositions.