Fluorescence resonance energy transfer FRET study

Toth PT, Ren D, Miller RJ (2004) Regulation of CXCR4 receptor dimerization by the chemokine SDF-lalpha and the HIV-1 coat protein gpl20 a fluorescence resonance energy transfer (FRET) study. J Pharmacol Exp Ther 310 8-17 Tran PB, Miller RJ (2005) HIV-1, chemokines and neurogenesis. Neurotox Res 8 149-158 Tran PB, Ren D, Veldhouse TJ, Miller RJ (2004) Chemokine receptors are expressed widely by embryonic and adult neural progenitor cells. J Neurosci Res 76 20-34... 

Toth PT, Ren D, Miller RJ. Regulation of CXCR4 receptor dimerization by the chemokine SDF-lalpha and the HIV-1 coat protein gpl20 a fluorescence resonance energy transfer (FRET) study. J Pharmacol Exp Ther 2004 310(1) 8-17. 

The use of either pairs of differently fluorescent-labeled receptors or fluorescent-labeled receptors and fluorescent-labeled peptides allows fluorescence resonance energy transfer (FRET) studies. The prerequisite is that the used chromophores form a FRET pair. This means, when in close proximity, that fhe so-called donor, excited at a certain wavelength, transfers its radiation energy non-radiatively to the closely located acceptor chromophore. Emission at the acceptor s emission wave-... 

Xu QH, Wang S, Korystov D, Mikhailovsky A, Bazan GC (2005) The fluorescence resonance energy transfer (FRET) gate a time-resolved study. Proc Natl Acad Sci USA 102 530-535... 

The intersubunit rotation is required for translocation as ribosomes trapped in the nonrotated state by an engineered intersubunit disulfide bridge fail in tRNA-mRNA movement. Real-time observation of intersubunit movement by fluorescence resonance energy transfer (FRET) showed that intersubunit movement occurs concomitantly with hybrid state formation, and that the rotated state can be trapped by the antibiotic viomycin. Similarly to the fluctuation of tRNAs between classical and hybrid states, single-molecule studies have detected spontaneous intersubunit movement where the 3 OS subunit fluctuates between a rotated... 

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]... 

Fluorescence resonance energy transfer (FRET) is a spectroscopic means of obtaining distance information over a range up to 80 A in solution. It is based on the dipolar coupling between the electronic transition moments of a donor and acceptor fluorophore attached at known positions on the RNA species of interest. It can be applied in ensembles of molecules, either by steady-state fluorescence or by lifetime measurements, but it is also very appropriate for single-molecule studies. In addition to the provision of distance information, recent studies have emphasized the orientation dependence of energy transfer. 

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