Cooling of radiative quantum dot excitons by THz-radiation

Chaos synchronization of delayed quantum dot light emitting diode has been studied theortetically which are coupled via the unidirectional and bidirectional. at synchronization of chaotic, The dynamics is identical with delayed optical feedback for those coupling methods. Depending on the coupling parameters and delay time the system exhibits complete synchronization, . Under proper conditions, the receiver quantum dot light emitting diode can be satisfactorily synchronized with the transmitter quantum dot light emitting diode due to the optical feedback effect.

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Vertical-cavity emitting devices with quantum-dot structures

Uspekhi Fizicheskih Nauk ◽

10.3367/ufnr.0171.200108d.0855 ◽

2001 ◽

Vol 171 (8) ◽

pp. 855

Author(s):

Viktor M. Ustinov ◽

N.A. Maleev ◽

Aleksei E. Zhukov ◽

A.R. Kovsh ◽

A.V. Sakharov ◽

...

Keyword(s):

Quantum Dot ◽

Vertical Cavity

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Quantum Dot Bioconjugates as Energy Donors in Fluorescence Resonance Energy Transfer Assays

MRS Proceedings ◽

10.1557/proc-773-n7.9 ◽

2003 ◽

Vol 773 ◽

Author(s):

Aaron R. Clapp ◽

Igor L. Medintz ◽

J. Matthew Mauro ◽

Hedi Mattoussi

Keyword(s):

Energy Transfer ◽

Quantum Dot ◽

Organic Dyes ◽

Resonance Energy Transfer ◽

Resonance Energy ◽

Genetically Engineered ◽

Molar Ratio ◽

Binding Assays ◽

Specific Sequence ◽

Donor Acceptor

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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