Resonance energy transfer as a monitor of membrane protein domain segregation: application to the aggregation of bacteriorhodopsin reconstituted into phospholipid vesicles

Biochemistry ◽  
1984 ◽  
Vol 23 (26) ◽  
pp. 6445-6452 ◽  
Author(s):  
C. A. Hasselbacher ◽  
Terry L. Street ◽  
T. G. Dewey
Keyword(s):  
Energy Transfer ◽  
Membrane Protein ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Protein Domain ◽  
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.

scholarly journals Fast slow folding of an Outer Membrane Porin

2021 ◽  
Author(s):  
Eve E. Weatherill ◽  
Monifa A. Fahie ◽  
David P. Marshall ◽  
Rachel A. Andvig ◽  
Matthew R. Cheetham ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Single Molecule ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Globular Proteins ◽  
Protein G ◽  
Outer Membrane Porin ◽  
Unfolded State

AbstractIn comparison to globular proteins, the spontaneous folding and insertion of β-barrel membrane proteins is surprisingly slow, typically occurring on the order of minutes. Using single-molecule Förster Resonance Energy Transfer to report on the folding of fluorescently-labelled Outer Membrane Protein G we measured the real-time insertion of a β-barrel membrane protein from an unfolded state. Folding events were rare, and fast (<20 ms); occurring immediately upon arrival at the membrane. This combination of infrequent, but rare, folding resolves this apparent dichotomy between slow ensemble kinetics, and the typical timescales of biomolecular folding.

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