scholarly journals Theory of coherent resonance energy transfer

2008 ◽  
Vol 129 (10) ◽  
pp. 101104 ◽  
Author(s):  
Seogjoo Jang ◽  
Yuan-Chung Cheng ◽  
David R. Reichman ◽  
Joel D. Eaves
2019 ◽  
Vol 33 (24) ◽  
pp. 1950281
Author(s):  
Xiaogang Bai ◽  
Haiming Zhang

The coherent energy transfer efficiency of a pair of two-level atoms is studied theoretically and its mathematical expression has been deduced. The problem of atoms coherent energy transfer theory is treated by quantum perturbation theory and equivalent method replacing atomic dipole field with light field of the same frequency. The detuning between the donor atom transition frequency and the acceptor atom transition frequency has been studied in the theory. With the increase of the detuning of the two-atomic transition frequency, the energy transfer efficiency decays rapidly. In the case of two-atomic transition frequency resonance, the coherent resonance energy transfer efficiency is directly proportional to the square of the sine of the minus three power of the distance between two atoms and the energy transfer efficiency is periodically decaying over time. The coherent resonance energy transfer efficiency is inversely proportional to the six power of the distance between the two atoms in the first-order approximation.


2003 ◽  
Vol 773 ◽  
Author(s):  
Aaron R. Clapp ◽  
Igor L. Medintz ◽  
J. Matthew Mauro ◽  
Hedi Mattoussi

AbstractLuminescent CdSe-ZnS core-shell quantum dot (QD) bioconjugates were used as energy donors in fluorescent resonance energy transfer (FRET) binding assays. The QDs were coated with saturating amounts of genetically engineered maltose binding protein (MBP) using a noncovalent immobilization process, and Cy3 organic dyes covalently attached at a specific sequence to MBP were used as energy acceptor molecules. Energy transfer efficiency was measured as a function of the MBP-Cy3/QD molar ratio for two different donor fluorescence emissions (different QD core sizes). Apparent donor-acceptor distances were determined from these FRET studies, and the measured distances are consistent with QD-protein conjugate dimensions previously determined from structural studies.


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