Two-step FRET as a tool for probing the amyloid state of proteins

Volume: 294, Pages: 111675 - 111675
Published: Nov 1, 2019
Abstract
Amyloid fibrils, a special class of protein aggregates with a core β-sheet structure, are currently associated with a number of human disorders. The fluorescence-based techniques play essential role in detection and structural characterization of amyloid assemblies. The amyloid-sensing potential of the two-step Förster resonance energy transfer has been assessed using the three-chromophore system containing a benzothiazole dye Thioflavin T, a...
Paper Details
Title
Two-step FRET as a tool for probing the amyloid state of proteins
Published Date
Nov 1, 2019
Volume
294
Pages
111675 - 111675
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