Fluorescence resonance energy transfer experiments

Single lanthanide-doped oxide nanoparticles as donors in fluorescence resonance energy transfer experiments. J. Phys. Chem. 2006 110 19264-19270. 88. 

Table 4.2 Dye pairs used in single molecule fluorescence resonance energy transfer experiments ...

This breadth of reactivity necessitates understanding and control of selectivity. To this end, Sohn and Ihee have conducted fluorescence resonance energy transfer experiments with a range of catalysts, with specially designed alkenes, allenes, and alkynes that are tethered to a dye (Figure 2.12). When the ruthenium complex coordinates the alkene/allene/alkyne, the fluorescence is quenched. Catalysts studied included Mol, Gl, G2, GHl, and GH2 rate constants and thermodynamic parameters were obtained in each case (Table 2.8). These experiments showed that catalyst systems react... 

Figure 14. FRET (fluorescence resonance energy transfer) experiment between a surface-attached donor dye-labeled probe strand and an acceptor dye-labeled target strand from solution, Shown are the angular scans of the reflectivities and of the fluorescence emission of the donor dye before and after hybridization, as well as, after denaturing the hybrid. While the reflectivities are virtually identical the fluorescence shows a strong enhancement at surface plasmon resonance (—) which is completely quenched after hybridization (—), however, can be fully recovered upon the dissociation of the hybrid (..).

The possibility to carry out conformational studies of peptides at low concentrations and in the presence of complex biological systems represents a major advantage of fluorescence spectroscopy over other techniques. Fluorescence quantum yield or lifetime determinations, anisotropy measurements and singlet-singlet resonance energy transfer experiments can be used to study the interaction of peptides with lipid micelles, membranes, proteins, or receptors. These fluorescence techniques can be used to determine binding parameters and to elucidate conformational aspects of the interaction of the peptide with a particular macro-molecular system. The limited scope of this chapter does not permit a comprehensive review of the numerous studies of this kind that have been carried and only a few general aspects are briefly discussed here. Fluorescence studies of peptide interactions with macromolecular systems published prior to 1984 have been reviewed. 

Chirio-Lebrun MC, Prats M. Fluorescence resonance energy transfer (FRET) theory and experiments. Biochemical Education 1998, 26, 320-323. 

The elucidation of the structure, dynamics and self assembly of biopolymers has been the subject of many experimental, theoretical and computational studies over the last several decades. [1, 2] More recently, powerful singlemolecule (SM) techniques have emerged which make it possible to explore those questions with an unprecedented level of detail. [3-55] SM fluorescence resonance energy transfer (FRET), [56-60] in particular, has been established as a unique probe of conformational structure and dynamics. [26-55] In those SM-FRET experiments, one measures the efficiency of energy transfer between a donor dye molecule and an acceptor dye molecule, which label specific sites of a macromolecule. The rate constant for FRET from donor to acceptor is assumed to be given by the Forster theory, namely [59,61-64]... 

Forster s theory [1], has enabled the efficiency of EET to be predicted and analyzed. The significance of Forster s formulation is evinced by the numerous and diverse areas of study that have been impacted by his paper. This predictive theory was turned on its head by Stryer and Haugland [17], who showed that distances in the range of 2-50 nm between molecular tags in a protein could be measured by a spectroscopic ruler known as fluorescence resonance energy transfer (FRET). Similar kinds of experiments have been employed to analyze the structure and dynamics of interfaces in blends of polymers. 

Optical experiments such as fluorescence resonance energy transfer can give slructural/dynamic information about length scales of up to 100 A that are not accessible in NMR experiments... 

Combination of fluorescence resonance energy transfer with stopped flow experiments helped to resolve submillisecond events in die folding of ACBP, This approaeh has allowed the eharaeterization of the kinetics and stability of a transient intermediate populated on the 100-ps time seale. Thus, intermediate states between native and totally denatured do exists in ACBP as it is observed for other proteins sueh as apomyoglobin. 

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