Spectra FRET: A Fluorescence Resonance Energy Transfer Method in Live Cells

Bykova, Ekaterina A.; Zheng, Jie

doi:10.1007/978-0-387-88722-7_4

Cited by 3 publications

(3 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The background emission of RBM5-143 at 625 nm observed at the donor excitation (λ exc = 455 nm) is indicative of an excitation cross-talk (or acceptor excitation bleed-through, AEB), a phenomenon related to the overlap of the donor and acceptor absorption spectra. This phenomenon, together with the related emission cross-talk (or donor emission bleed-through, DEB), arising from the overlap of the donor and acceptor emission spectra 32 must be carefully considered in the design of ratiometric experiments based on the development of the FRET effect. In contrast, ratiometric experiments based on FRET attenuation 21,22,24 may benefit from the disappearance of these interferences.…”

Section: Optimization Of the Spaac Reaction From Rbm5-159mentioning

confidence: 99%

“…This parameter was estimated following a reported protocol. 32 The AEB for the different donor-acceptor pairs were calculated as the percentage between the slopes of the plots of absorbance at the λ ex vs. integrated fluorescence intensity corresponding to the calculated AEB spectra and to those corresponding to F d DAðTotÞ (integrated fluorescence of the non-deconvoluted spectra, being (eqn ( 7)).…”

Section: Composite Spectra Deconvolutionmentioning

confidence: 99%

See 1 more Smart Citation

Synthesis and characterization of bichromophoric 1-deoxyceramides as FRET probes

et al. 2021

View full text Add to dashboard Cite

show abstract

Section: Optimization Of the Spaac Reaction From Rbm5-159mentioning

confidence: 99%

Section: Composite Spectra Deconvolutionmentioning

confidence: 99%

Synthesis and characterization of bichromophoric 1-deoxyceramides as FRET probes

et al. 2021

View full text Add to dashboard Cite

show abstract

“…In biochemistry, the socalled FRET, is used for analysing conformational substates of biological macromolecules and for relating their structure to the function. [1,2] Moreover, FRET is used to follow molecular dynamics in live cells. Excitation energy transfer has been studied in conjugated organic materials in order to improve optoelectronic devices.…”

Section: Introductionmentioning

confidence: 99%

Effect of External Pressure on the Excitation Energy Transfer from [Cr(ox)₃]³⁻ to [Cr(bpy)₃]³⁺ in [Rh_1−xCr_x(bpy)₃][NaM_1−yCr_y(ox)₃]ClO₄

2010

View full text Add to dashboard Cite

Resonant excitation energy transfer from [Cr(ox)(3)](3-) to [Cr(bpy)(3)](3+) in the doped 3D oxalate networks [Rh(1-x)Cr(x)(bpy)(3)][NaM(III) (1-y)Cr(y)(ox)(3)]ClO(4) (ox=C(2)O(4) (-), bpy=2,2'-bipyridine, M=Al, Rh) is due to two types of interaction, namely super exchange coupling and electric dipole-dipole interaction. The energy transfer probability for both mechanisms is proportional to the spectral overlap of the (2)E→(4)A(2) emission of the [Cr(ox)(3)](3-) donor and the (4)A(2)→(2)T(1) absorption of the [Cr(bpy)(3)](3+) acceptor. The spin-flip transitions of (pseudo-)octahedral Cr(3+) are known to shift to lower energy with increasing pressure. Because the shift rates of the two transitions in question differ, the spectral overlap between the donor emission and the acceptor absorption is a function of applied pressure. For [Rh(1-x)Cr(x)(bpy)(3)][NaM(1-y)Cr(y)(ox)(3)]ClO(4) the spectral overlap is thus substantially reduced on increasing pressure from 0 to 2.5 GPa. As a result, the energy transfer probability decreases with increasing pressure as evidenced by a decrease in the relative emission intensity from the [Cr(bpy)(3)](3+) acceptor.

show abstract

Dynamic tuneable G protein-coupled receptor monomer-dimer populations

et al. 2018

View full text Add to dashboard Cite

G protein-coupled receptors (GPCRs) are the largest class of membrane receptors, playing a key role in the regulation of processes as varied as neurotransmission and immune response. Evidence for GPCR oligomerisation has been accumulating that challenges the idea that GPCRs function solely as monomeric receptors; however, GPCR oligomerisation remains controversial primarily due to the difficulties in comparing evidence from very different types of structural and dynamic data. Using a combination of single-molecule and ensemble FRET, double electron–electron resonance spectroscopy, and simulations, we show that dimerisation of the GPCR neurotensin receptor 1 is regulated by receptor density and is dynamically tuneable over the physiological range. We propose a “rolling dimer” interface model in which multiple dimer conformations co-exist and interconvert. These findings unite previous seemingly conflicting observations, provide a compelling mechanism for regulating receptor signalling, and act as a guide for future physiological studies.

show abstract

Spectra FRET: A Fluorescence Resonance Energy Transfer Method in Live Cells

Cited by 3 publications

References 24 publications

Synthesis and characterization of bichromophoric 1-deoxyceramides as FRET probes

Synthesis and characterization of bichromophoric 1-deoxyceramides as FRET probes

Effect of External Pressure on the Excitation Energy Transfer from [Cr(ox)₃]³⁻ to [Cr(bpy)₃]³⁺ in [Rh_1−xCr_x(bpy)₃][NaM_1−yCr_y(ox)₃]ClO₄

Dynamic tuneable G protein-coupled receptor monomer-dimer populations

Contact Info

Product

Resources

About

Spectra FRET: A Fluorescence Resonance Energy Transfer Method in Live Cells

Cited by 3 publications

References 24 publications

Synthesis and characterization of bichromophoric 1-deoxyceramides as FRET probes

Synthesis and characterization of bichromophoric 1-deoxyceramides as FRET probes

Effect of External Pressure on the Excitation Energy Transfer from [Cr(ox)3]3− to [Cr(bpy)3]3+ in [Rh1−xCrx(bpy)3][NaM1−yCry(ox)3]ClO4

Dynamic tuneable G protein-coupled receptor monomer-dimer populations

Contact Info

Product

Resources

About

Effect of External Pressure on the Excitation Energy Transfer from [Cr(ox)₃]³⁻ to [Cr(bpy)₃]³⁺ in [Rh_1−xCr_x(bpy)₃][NaM_1−yCr_y(ox)₃]ClO₄