Rhodopsin in reconstituted phospholipid vesicles. 2. Rhodopsin-rhodopsin interactions detected by resonance energy transfer

Biochemistry ◽  
1983 ◽  
Vol 22 (1) ◽  
pp. 206-213 ◽  
Author(s):  
Hamutal Borochov-Neori ◽  
P. A. George Fortes ◽  
Mauricio Montal
Keyword(s):  
Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Phospholipid Vesicles

scholarly journals Dibucaine interaction with phospholipid vesicles. A resonance energy-transfer study

1990 ◽  
Vol 189 (2) ◽  
pp. 387-393 ◽  
Author(s):  
Ana COUTINHO ◽  
Julia COSTA ◽  
Joaquim L. FARIA ◽  
Mario N. BERBERAN-SANTOS ◽  
Manuel J. E. PRIETO
Keyword(s):  
Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Phospholipid Vesicles ◽  
Transfer Study

scholarly journals Interaction of cholesterol-crystallization-promoting proteins with vesicles

1995 ◽  
Vol 305 (1) ◽  
pp. 93-96 ◽  
Author(s):  
M A C de Bruijn ◽  
B G Goldhoorn ◽  
A I M Zijlstra ◽  
G N J Tytgat ◽  
A K Groen
Keyword(s):  
Energy Transfer ◽  
Concanavalin A ◽  
Binding Proteins ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Phospholipid Vesicles ◽  
Human Bile ◽  
Induced Crystallization

In this study, the interaction of mucin and concanavalin A-binding proteins isolated from human bile with cholesterol/phospholipid vesicles was investigated. Using resonance energy transfer assays originally developed by Struck, Hoekstra and Pagano [(1981) Biochemistry 20, 4093-4099], no significant protein-induced fusion or aggregation of vesicles was demonstrated. Instead of fusion, these proteins induced destabilization of cholesterol/phospholipid vesicles, as monitored by release of entrapped carboxyfluorescein. A good correlation (rho = 0.81) was obtained between the extent of leakage and the nucleation-promoting activity of the concanavalin A-binding proteins. We conclude that aggregation or fusion of cholesterol/phospholipid vesicles is not an obligatory step in cholesterol crystallization. Biliary protein-induced crystallization seems to be preceded by vesicle disruption.

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

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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