Photoswitchable Förster resonance energy transfer (FRET) within a heterometallic Ir-Pt macrocycle

Yi Qin1, Li-Jun Chen1, Ying Zhang2

  • 1Shanghai Key Laboratory of Green Chemistry and Chemical Processes, School of Chemistry and Molecular Engineering, East China Normal University, 3663 North Zhongshan Road, Shanghai 200062, P. R. China. lijun.chen@sydney.edu.au lxu@chem.ecnu.edu.cn hbyang@chem.ecnu.edu.cn.

Chemical Communications (Cambridge, England)
|August 29, 2019
PubMed

Related Concept Videos

Förster Resonance Energy Transfer (FRET)06:39

Förster Resonance Energy Transfer (FRET)

Förster resonance energy transfer (FRET) is a phenomenon used to investigate close-range biochemical interactions. In FRET, a donor photoluminescent molecule can non-radiatively transfer energy to an acceptor molecule if their respective emission and absorbance spectra overlap. The amount of energy transferred—and consequently the overall emission of sample—depends on the proximity of an acceptor-donor pair of photoluminescent molecules. FRET analysis is combined with other...
46.0K
Visualizing Cellular Gibberellin Levels Using the nlsGPS1 Förster Resonance Energy Transfer (FRET) Biosensor08:53

Visualizing Cellular Gibberellin Levels Using the nlsGPS1 Förster Resonance Energy Transfer (FRET) Biosensor

Gibberellin Perception Sensor 1 (GPS1) is the first Förster resonance energy transfer-based biosensor for measuring the cellular levels of gibberellin phytohormones with a high spatiotemporal resolution. This protocol reports on the method to visualize and quantify cellular gibberellin levels using the genetically encoded nlsGPS1 biosensor in Arabidopsis hypocotyls and root...
11.4K
Time-Resolved Forster Resonance Energy Transfer for Monitoring Protein Phosphorylation in Cells05:13

Time-Resolved Forster Resonance Energy Transfer for Monitoring Protein Phosphorylation in Cells

This video describes the time-resolved Förster resonance energy transfer or TR-FRET assay to determine endogenous protein phosphorylation with the help of donor and acceptor fluorophores tagged on antibodies specific to a test protein. This technique is designed to measure the phosphorylation of test proteins in cell...
550
Quantitative FRET (Förster Resonance Energy Transfer) Analysis for SENP1 Protease Kinetics Determination16:02

Quantitative FRET (Förster Resonance Energy Transfer) Analysis for SENP1 Protease Kinetics Determination

A novel method involving quantitative analysis of FRET (Förster Resonance Energy Transfer) signals is described for studying enzyme kinetics. KM and kcat were obtained for the hydrolysis of the catalytic domain of SENP1 (SUMO/Sentrin specific protease 1) to pre-SUMO1 (Small Ubiquitin-like MOdifier). The general principles of this quantitative-FRET-based protease kinetic study can be applied to other...
19.7K
Förster Resonance Energy Transfer Measurements in Living Plant Cells06:53

Förster Resonance Energy Transfer Measurements in Living Plant Cells

A protocol is provided for setting up a standard confocal laser-scanning microscope for in vivo Förster resonance energy transfer measurements, followed by data...
3.3K
Förster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features07:09

Förster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features

The study details the methodology of FRET mapping including the selection of labeling sites, choice of dyes, acquisition, and data analysis. This methodology is effective at determining binding sites, conformational changes, and dynamic motions in protein systems and is most useful if performed in conjunction with existing 3-D structural...
3.0K