Forster resonance energy transfer donor

Hildebrandt N, Charbonniere LJ, Lohmannsroben HG (2007) Time-resolved analysis of a highly sensitive forster resonance energy transfer immunoassay using terbium complexes as donors and quantum dots as acceptors. J Biomed Biotechnol 2007 79169... 

Liao F, Xie Y, Yang X et al (2009) Homogeneous noncompetitive assay of protein via Forster-resonance-energy-transfer with tryptophan residue(s) as intrinsic donor(s) and fluorescent ligand as acceptor. Biosens Bioelectron 25 112-117... 

Day RN, Booker CF, Periasamy A (2008) Characterization of an improved donor fluorescent protein for Forster resonance energy transfer microscopy. J Biomed Opt 13 031203. doi 10.1117/1111.2939094... 

The lifetime of the excited state of fluorophores may be altered by physical and biochemical properties of its environment. Fluorescence lifetime imaging microscopy (FLIM) is thus a powerful analytical tool for the quantitative mapping of fluorescent molecules that reports, for instance, on local ion concentration, pH, and viscosity, the fluorescence lifetime of a donor fluorophore, Forster resonance energy transfer can be also imaged by FLIM. This provides a robust method for mapping protein-protein interactions and for probing the complexity of molecular interaction networks. 

Forster resonance energy transfer (FRET) is a form of quenching. For a fluorophore (donor) to be quenched by another molecule (acceptor), three criteria must be met ... 

A detailed theory of energy transfer by the Coulombic mechanism was developed by Forster, so the process is often referred to as Forster resonance energy transfer (FRET). According to the Forster theory, the probability of Coulombic energy transfer falls off inversely with the sixth power of the distance between the donor and the acceptor. For... 

The Forster resonance energy transfer can be used as a spectroscopic ruler in the range of 10-100 A. The distance between the donor and acceptor molecules should be constant during the donor lifetime, and greater than about 10 A in order to avoid the effect of short-range interactions. The validity of such a spectroscopic ruler has been confirmed by studies on model systems in which the donor and acceptor are separated by well-defined rigid spacers. Several precautions must be taken to ensure correct use of the spectroscopic ruler, which is based on the use of Eqs (9.1) to (9.3) ... 

Fluorescence (or Forster) resonance energy transfer (FRET) is a process by which energy is transferred nonradiatively from an excited donor to a nearby ground state acceptor. This process arises due to dipole-dipole interactions and is... 

A complete FRET (Forster resonance energy transfer) system based on chlorophyll in the pores of FSM materials was accomplished by Kuroda s group.149,150 They first functionalized the FSM samples with 3-aminopropyl groups to guarantee an ideal position of the macroscopic chlorin units (in the pore center) and prevent their denaturation. Then they ligated chlorophyll derivatives that possess 3-(triethoxy-silyl)-A-methylpropan-l -amine groups to the pore walls. Zinc (for the FRET donor) and copper (for the FRET acceptor) were chosen as the central ions of the chlorins, which made it possible to initiate and record an efficient FRET process (Fig. 3.14). 

QDs have been also used extensively as efficient donors in the development of Forster resonance energy transfer (FRET) systems. The key developments and most recent applications in chemical analysis using such QDs-based strategies are reviewed below. 

Medintz IL, Clapp AR, Melinger JS, Deschamps JR, Mattoussi H. A reagentless biosensing assembly based on quantum dot donor Forster resonance energy transfer. Adv. Mat. 2005 17 2450-2455. 

In the case of Forster resonance energy transfer (FRET) [13], i.e. energy transfer by the dipole-dipole mechanism, and for randomly oriented donor-acceptor pairs, the depolarization after one transfer step (ensemble average) is almost complete [27]. For this reason, fluorescence anisotropy is a good indicator of energy transfer between identical fluorophores, hence of relative distances. Existence of efficient FRET may therefore reflect an association process. 

It is useful in discussion of weak coupling between nanostructures to remember the nonradiative mechanism of Forster resonant energy transfer from an excited molecule (a donor) to some other molecule (an acceptor) which can be in the ground or in an excited state. The probability of such a transfer is determined by the Coulomb nonretarded (instantaneous) dipole-dipole interaction between molecules and is proportional to Rp/R6 where Rp is the Forster radius and R is the distance between molecules. For organic materials the Forster radius is usually about several nanometers and strongly depends on the overlapping... 

In fluorescence resonance energy transfer, also called Forster resonance energy transfer FRET), an excited fluorophore in one part of a molecule (the donor) has its fluorescence... 

An efficient Forster resonance energy transfer takes place from the donor PVK to the acceptor, the silicon nanoparticles. This makes the composite a promising material for polymer inorganic hybrid light-emitting diodes [90]. 

Forster Resonance Energy Transfer. This is a single-step, radzafion/css transfer of electronic excitation. This t5zpe of energy transfer depends in part on the distance between the donor and acceptor but can take place over distances of up to 100 A. Efficient Forster transfer also requires a good overlap of the emission spectnun of the donor and the absorption spectrum of the acceptor. 

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