Spectroscopy resonance energy transfer

Clegg RM (1996) Fluorescence resonance energy transfer. In Wang XF, Flerman B (eds) Fluorescence imaging spectroscopy and microscopy. John Wiley, New York, pp 179-252... 

Clegg, R. M. (1996). Fluorescence resonance energy transfer. In Fluorescence Imaging. Spectroscopy and Microscopy. Vol. 137. (Wang, X. F. and Herman, B., eds.). John Wiley Sons, New York, pp. 179-252. 

Young, S. H., Dong, W. J. and Jacobs, R. R. (2000). Observation of a partially opened triple-helix conformation in l->3-beta-glucan by fluorescence resonance energy transfer spectroscopy. J. Biol. Chem. 275, 11874-11879. 

Zheng, J. (2006). Spectroscopy-based quantitative fluorescence resonance energy transfer analysis. Methods Mol. Biol. 337, 65-77. 

Cheung H. C. (1991) Resonance Energy Transfer, in Larowicz J. R. (Ed.), Topics in Fluorescence Spectroscopy, Vol. 2, Principles, Plenum Press, New York, pp. 127-176. 

The molecular interaction of cytochrome c and cardiolipin has been extensively studied. A mode of the interaction has been confirmed to be both electrostatic and hydrophobic, by using infrared spectroscopy (Choi and Swanson, 1995), fluorescence resonance energy transfer method (Rytdmaa and Kinnunen, 1994), protease digestion (de Jongh et al., 1995), cyclic voltammetry (Salamon and ToUin, 1997), deuterium and phosphorus NMR measurements (Spooner et al., 1993), and surface plasmon resonance spectroscopy (Salamon and Tollin, 1996). 

Other fluorescence-based methods to investigate target-ligand interactions use fluorescence correlation spectroscopy (FCS) or fluorescence resonance energy transfer (FRET) [8, 12, 46]. 

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. 

New boxed applications include an arsenic biosensor (Chapter 0). microcantilevers to measure attograms of mass (Chapter 2), molecular wire (Chapter 14), a fluorescence resonance energy transfer biosensor (Chapter 19), cavity ring-down spectroscopy for ulcer diagnosis (Chapter 20), and environmental mercury analysis by atomic fluorescence (Chapter 21). 

Abbreviations AOD, Acousto-optical deflection BCB, bisbenzyocyclobutadiene CCD, indirect contact conductivity detection CL, chemiluminescence ECD, electron capture detector FCS, fluorescence correlation spectroscopy FRET, fluorescence resonance energy transfer ICCD, integrated contact conductivity detection GMR, giant magnetoresistive LED-CFD, light emitting diode confocal fluorescence detector LIF, laser-induced fluorescence LOD, limit of detection MALDI, matrix-assisted laser desorption ionization PDMS, poly(dimethylsiloxane) PMMA, poly(methylmetha-crylate) SPR, surface plasmon resonance SVD, sinusoidal voltammetric detection TLS, thermal lens spectroscopy. 

Dosremedios CG, Moens PDJ. Fluorescence resonance energy-transfer spectroscopy is arehable ruler for measuring structural changes in proteins. Dispelling the problem of the unknown orientation factor. Journal of Structural Biology 1995, 115, 175-185. 

The fluorescence lifetime of a fluorophore is highly sensitive to its molecular environment. Many macromolecular events, such as rotational diffusion, resonance-energy transfer, and dynamic quenching, occur on the same timescale as the fluorescence decay. Thus, time-resolved fluorescence spectroscopy can be used to investigate these processes and gain insight into the chemical surroundings of the fluorophore. 

FIGURE 4.1 Assays commonly used in GPCR research. SPA = scintillation proximity assay FP = fluorescence polarization TR-FRET = time-resolved fluorescence resonance energy transfer FCS = fluorescence correlation spectroscopy SeAP = secreted alkaline phosphate TF = transcription factor EFC = enzyme fragment complementation DMR = dynamic mass redistribution CDS = cellular dielectric spectroscopy. 

Fluorescence-based detection methods are the most commonly used readouts for HTS as these readouts are sensitive, usually homogeneous and can be readily miniaturised, even down to the single molecule level.7,8 Fluorescent signals can be detected by methods such as fluorescence intensity (FI), fluorescence polarisation (FP) or anisotropy (FA), fluorescence resonance energy transfer (FRET), time-resolved fluorescence resonance energy transfer (TR-FRET) and fluorescence intensity life time (FLIM). Confocal single molecule techniques such as fluorescence correlation spectroscopy (FCS) and one- or two-dimensional fluorescence intensity distribution analysis (ID FID A, 2D FIDA) have been reported but are not commonly used. 

A = agar plate-based assay S = solution-based assay FRET = fluorescence resonance energy transfer FP = fluorescence polarization FCS = fluorescence correlation spectroscopy... 

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