Supramolecular nanostructured materials, displaying Förster resonance energy transfers (FRET) signals, have become the focus of interest for many researchers across globe. FRET based supramolecular systems extended applications in areas as diverse materials science, biochemistry, analytical chemistry, and nanomedicine. The non-covalent phenomena operating frameworks depends on factors such wide...

Proteases are closely associated with many pathological conditions. Efficient detection of protease activity may be useful for diagnosis, prognosis, and the development new therapeutic biomolecules. Fluorescent Resonance Energy Transfer (FRET) is defined as non-radioactive energy transfer that occurs between two fluorophores. proteins widely used in FRET biosensors because they can genetically ...

Fluorescence Resonance Energy Transfer (FRET) using fluorescent protein variants is widely used to study biochemical processes in living cells. FRET detection by fluorescence lifetime measurements is the most direct and robust method to measure FRET. The traditional cyan-yellow fluorescent protein based FRET pairs are getting replaced by green-red fluorescent protein variants. The green-red pai...

FRET has emerged as an important tool for studying intracellular processes and interactions between biomolecules. Intracellular donor and acceptor molecules are distributed in individual organelles that usually have complex non-continuous shape. Consequently, background pixels arising from fluorophore-free regions of the cell are proximal to FRET-positive pixels, leading to systemic errors in t...

The Structured Illumination (SI)-based Super Resolution Fluorescence Resonance Energy Transfer (SR-FRET) imaging technique, known as SISR-FRET, enables the investigation of molecular structures and functions in cellular organelles by resolving sub-diffraction FRET signals within living cells. microscopy offers unique advantages for quantitatively detecting dynamic interactions spatial distribut...

Fluorescence resonance energy transfer (FRET) microscopy is a powerful tool for imaging the interactions between fluorescently tagged proteins in two-dimensions. For FRET microscopy to reach its full potential, it must be able to image more than one pair of interacting molecules and image degradation from out-of-focus light must be reduced. Here we extend our previous work on the application of...

We have developed a novel method for multi-color spectral FRET analysis which is used to study a system of three independent FRET-based molecular sensors composed of the combinations of only three fluorescent proteins. This method is made possible by a novel routine for computing the 3-D excitation/emission spectral fingerprint of FRET from reference measurements of the donor and acceptor alone...

Förster resonance energy transfer (FRET) describes excitation energy exchange between two adjacent molecules typically in distances ranging from 2 to 10 nm. The process depends on dipole-dipole coupling of the molecules and its probability of occurrence cannot be proven directly. Mostly, fluorescence is employed for quantification as it represents a concurring process of relaxation of the excit...

A real-time assay system that allows monitoring of intracellular human enterovirus (HEV) protease activity was established using the principle of fluorescence resonance energy transfer (FRET). It was accomplished by engineering cells to constitutively express a genetically encoded FRET probe. The FRET-based probe was designed to contain an enterovirus 71 3C protease (3C(pro)) cleavage motif fla...