Comment on ““Where does the fluorescing moiety reside in a carbon dot?” – Investigations based on fluorescence anisotropy decay and resonance energy transfer dynamics” by A. Das, D. Roy, C. K. De and P. K. Mandal, Phys. Chem. Chem. Phys., 2018, 20, 2251

2019 ◽  
Vol 21 (24) ◽  
pp. 13368-13369 ◽  
Author(s):  
Hem C. Joshi
Keyword(s):  
Physical Chemistry ◽  
Energy Transfer ◽  
Fluorescence Anisotropy ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Chem Phys ◽  
Chemical Physics ◽  
Fluorescence Anisotropy Decay ◽  
Anisotropy Decay ◽  
Phys Chem Chem Phys

In a recent paper published in Physical Chemistry Chemical Physics (Phys. Chem. Chem. Phys., 2018, 20, 2251–2259), Förster resonance energy transfer (FRET) between carbon dots and rhodamine 123 has been reported.

scholarly journals “Where does the fluorescing moiety reside in a carbon dot?” – Investigations based on fluorescence anisotropy decay and resonance energy transfer dynamics

2018 ◽  
Vol 20 (4) ◽  
pp. 2251-2259 ◽  
Author(s):  
Ananya Das ◽  
Debjit Roy ◽  
Chayan K. De ◽  
Prasun K. Mandal
Keyword(s):  
Energy Transfer ◽  
Fluorescence Anisotropy ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Fluorescence Anisotropy Decay ◽  
Carbon Dot ◽  
Anisotropy Decay ◽  
High Fluorescence ◽  
Very High

It has been shown recently that aggregated dyes are responsible for very high fluorescence in a carbon dot (CD). Location of the fluorescing unit in a carbon dot could be shown.

Molecular probes: insights into design and analysis from computational and physical chemistry

2008 ◽  
Vol 36 (1) ◽  
pp. 46-50 ◽  
Author(s):  
Felicity L. Mitchell ◽  
Gabriel E. Marks ◽  
Elena V. Bichenkova ◽  
Kenneth T. Douglas ◽  
Richard A. Bryce
Keyword(s):  
Physical Chemistry ◽  
Energy Transfer ◽  
Experimental Approach ◽  
Fluorescent Protein ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Molecular Probes ◽  
Green Fluorescent ◽  
Nanoscale Level

The application of new molecular diagnostics to probe cellular process in vivo is leading to a greater understanding of molecular cytology at a sub-nanoscale level and is opening the way to individualized medicines. We review here three distinct fluorescence-based molecular probes, HyBeacons™, split-probe exciplexes and GFP (green fluorescent protein)-based FRET (fluorescence resonance energy transfer) systems. Through this, we highlight the insights into the mechanism and design that a combined computational and experimental approach can yield.

Tryptophan mutants of human C5a anaphylatoxin: A fluorescence anisotropy decay and energy transfer study

1993 ◽  
Vol 46 (3) ◽  
pp. 237-248 ◽  
Author(s):  
M. Federwisch ◽  
A. Wollmer ◽  
M. Emde ◽  
T. Stühmer ◽  
T. Melcher ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Fluorescence Anisotropy ◽  
Fluorescence Anisotropy Decay ◽  
Anisotropy Decay ◽  
C5a Anaphylatoxin ◽  
Transfer Study

scholarly journals Imaging of fluorescence anisotropy during photoswitching provides a simple readout for protein self-association

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Namrata Ojha ◽  
Kristin H. Rainey ◽  
George H. Patterson
Keyword(s):  
Energy Transfer ◽  
Fluorescence Anisotropy ◽  
Fluorescent Proteins ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Living Cells ◽  
Energy Transfer Efficiency ◽  
Protein Oligomerization ◽  
Self Association ◽  
Fluorescent Molecules

AbstractMonitoring of protein oligomerization has benefited greatly from Förster Resonance Energy Transfer (FRET) measurements. Although donors and acceptors are typically fluorescent molecules with different spectra, homo-FRET can occur between fluorescent molecules of the same type if the emission spectrum overlaps with the absorption spectrum. Here, we describe homo-FRET measurements by monitoring anisotropy changes in photoswitchable fluorescent proteins while photoswitching to the off state. These offer the capability to estimate anisotropy in the same specimen during homo-FRET as well as non-FRET conditions. We demonstrate photoswitching anisotropy FRET (psAFRET) with a number of test chimeras and example oligomeric complexes inside living cells. We also present an equation derived from FRET and anisotropy equations which converts anisotropy changes into a factor we call delta r FRET (drFRET). This is analogous to an energy transfer efficiency and allows experiments performed on a given homo-FRET pair to be more easily compared across different optical configurations.

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