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- W2080367104 abstract "Free-solution, label-free molecular interactions were investigated with back-scattering interferometry in a simple optical train composed of a helium-neon laser, a microfluidic channel, and a position sensor. Molecular binding interactions between proteins, ions and protein, and small molecules and protein, were determined with high dynamic range dissociation constants ( K d spanning six decades) and unmatched sensitivity (picomolar K d 's and detection limits of 10,000s of molecules). With this technique, equilibrium dissociation constants were quantified for protein A and immunoglobulin G, interleukin-2 with its monoclonal antibody, and calmodulin with calcium ion Ca 2+ , a small molecule inhibitor, the protein calcineurin, and the M13 peptide. The high sensitivity of back-scattering interferometry and small volumes of microfluidics allowed the entire calmodulin assay to be performed with 200 picomoles of solute." @default.
- W2080367104 created "2016-06-24" @default.
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- W2080367104 date "2007-09-21" @default.
- W2080367104 modified "2023-10-18" @default.
- W2080367104 title "Free-Solution, Label-Free Molecular Interactions Studied by Back-Scattering Interferometry" @default.
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- W2080367104 doi "https://doi.org/10.1126/science.1146559" @default.
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