scholarly journals Probing Polytopic Membrane Protein–Substrate Interactions by Luminescence Resonance Energy Transfer

2016 ◽  
Vol 138 (11) ◽  
pp. 3806-3812 ◽  
Author(s):  
Monika Musial-Siwek ◽  
Marcie B. Jaffee ◽  
Barbara Imperiali
Keyword(s):  
Energy Transfer ◽  
Membrane Protein ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Substrate Interactions ◽  
Protein Substrate ◽  
Polytopic Membrane Protein

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.

Quantitative analysis of membrane protein–amphiphile interactions using resonance energy transfer

2003 ◽  
Vol 317 (2) ◽  
pp. 171-179 ◽  
Author(s):  
Valeria Levi ◽  
Juan P.F.C. Rossi ◽  
Pablo R. Castello ◽  
F.Luis González Flecha
Keyword(s):  
Energy Transfer ◽  
Quantitative Analysis ◽  
Membrane Protein ◽  
Resonance Energy Transfer ◽  
Resonance Energy

scholarly journals Fluorescence Resonance Energy Transfer Detection of Synaptophysin I and Vesicle-associated Membrane Protein 2 Interactions during Exocytosis from Single Live Synapses

2002 ◽  
Vol 13 (8) ◽  
pp. 2706-2717 ◽  
Author(s):  
Maria Pennuto ◽  
David Dunlap ◽  
Andrea Contestabile ◽  
Fabio Benfenati ◽  
Flavia Valtorta
Keyword(s):  
Energy Transfer ◽  
Membrane Protein ◽  
Fluorescence Resonance Energy Transfer ◽  
Hippocampal Neurons ◽  
Fluorescent Protein ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Time Lapse ◽  
Vesicle Membrane ◽  
Fluorescence Resonance

To investigate the molecular interactions of synaptophysin I and vesicle-associated membrane protein 2 (VAMP2)/synaptobrevin II during exocytosis, we have used time-lapse videomicroscopy to measure fluorescence resonance energy transfer in live neurons. For this purpose, fluorescent protein variants fused to synaptophysin I or VAMP2 were expressed in rat hippocampal neurons. We show that synaptophysin I and VAMP2 form both homo- and hetero-oligomers on the synaptic vesicle membrane. When exocytosis is stimulated with α-latrotoxin, VAMP2 dissociates from synaptophysin I even in the absence of appreciable exocytosis, whereas synaptophysin I oligomers disassemble only upon incorporation of the vesicle with the plasma membrane. We propose that synaptophysin I has multiple roles in neurotransmitter release, regulating VAMP2 availability for the solubleN-ethylmaleimide-sensitive factor attachment protein receptor complex and possibly participating in the late steps of exocytosis.

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