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Visualization of Surface-tethered Large DNA Molecules with a Fluorescent Protein DNA Binding Peptide
Published on: June 23, 2016
Molecular tripods showing fluorescence enhancement upon binding to streptavidin
Tae Woo Kim1, Hey Young Yoon, Jung-Hyun Park
1Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul 151-747, Korea.
Abstract:
We introduce a new approach to biotin-streptavidin assays based on a molecular tripod which consists of biotin, a fluorophore, and a quencher. The interaction between streptavidin and molecular tripods perturbs the ground-state quencher-fluorophore dimeric conformation in the absence of streptavidin and diminishes the intrinsic self-quenching of a quencher-fluorophore pair. The emission intensity of the molecular tripods plus streptavidin is 3.5-5.2 times that of molecular tripods in the absence of streptavidin.
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