The Kinetics of the Iodine2-catalyzed Positional Isomerism of Butene-1. The Resonance Energy of the Allyl Radical

1963 ◽  
Vol 85 (10) ◽  
pp. 1388-1389 ◽  
Author(s):  
Sidney W. Benson ◽  
A. N. Bose ◽  
P. Nangia
Keyword(s):  
Resonance Energy ◽  
Allyl Radical ◽  
Positional Isomerism ◽  
Kinetics Of

Iodine-Catalyzed Isomerization of Olefins. II. The Resonance Energy of the Allyl Radical and the Kinetics of the Positional Isomerization of 1-Butene

1964 ◽  
Vol 86 (24) ◽  
pp. 5420-5424 ◽  
Author(s):  
Kurt W. Egger ◽  
David M. Golden ◽  
Sidney W. Benson
Keyword(s):  
Resonance Energy ◽  
Allyl Radical ◽  
Positional Isomerization ◽  
Kinetics Of

Kinetics of the Structural Transition of Muscle Thin Filaments Observed by Fluorescence Resonance Energy Transfer†

Biochemistry ◽  
2004 ◽  
Vol 43 (33) ◽  
pp. 10739-10747 ◽  
Author(s):  
Yuji Shitaka ◽  
Chieko Kimura ◽  
Takayoshi Iio ◽  
Masao Miki
Keyword(s):  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Structural Transition ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Thin Filaments ◽  
Fluorescence Resonance ◽  
Kinetics Of

Nonextensive kinetics of fluorescence resonance energy transfer

2008 ◽  
Vol 129 (14) ◽  
pp. 144507 ◽  
Author(s):  
Olaf J. Rolinski ◽  
David J. S. Birch
Keyword(s):  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Fluorescence Resonance ◽  
Kinetics Of

Equilibrium constant for allyl radical recombination. Direct measurement of "allyl resonance energy"

1969 ◽  
Vol 91 (8) ◽  
pp. 2136-2137 ◽  
Author(s):  
David M. Golden ◽  
Norman A. Gac ◽  
Sidney W. Benson
Keyword(s):  
Equilibrium Constant ◽  
Direct Measurement ◽  
Resonance Energy ◽  
Allyl Radical ◽  
Radical Recombination

The dissociation of 3-chloro-1-butene and the resonance energy of the chloro-allyl radical

1973 ◽  
Vol 5 (1) ◽  
pp. 67-75 ◽  
Author(s):  
A. B. Trenwith
Keyword(s):  
Resonance Energy ◽  
Allyl Radical

Direct measurement of the kinetics of CBM9 fusion-tag bioprocessing using luminescence resonance energy transfer

2009 ◽  
Vol 25 (3) ◽  
pp. 874-881 ◽  
Author(s):  
Mojgan Kavoosi ◽  
A. Louise Creagh ◽  
Robin F. B. Turner ◽  
Douglas G. Kilburn ◽  
Charles A. Haynes
Keyword(s):  
Energy Transfer ◽  
Direct Measurement ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Fusion Tag ◽  
Kinetics Of

scholarly journals Unveiling the multi-step solubilization mechanism of single vesicles by detergents

2019 ◽  
Author(s):  
Paul A. Dalgarno ◽  
José Juan-Colás ◽  
Gordon J. Hedley ◽  
Lucas Piñeiro ◽  
Mercedes Novo ◽  
...  
Keyword(s):  
Real Time ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Correlation Spectroscopy ◽  
Optical Methods ◽  
Fluorescence Correlation ◽  
Ionic Detergent ◽  
Triton X ◽  
Kinetics Of ◽  
Single Vesicle

AbstractThe solubilization of membranes by detergents is critical for many technological applications and has become widely used in biochemistry research to induce cell rupture, extract cell constituents, and to purify, reconstitute and crystallize membrane proteins. The thermodynamic details of solubilization have been extensively investigated, but the kinetic aspects remain poorly understood. Here we used a combination of single-vesicle Förster resonance energy transfer (svFRET), fluorescence correlation spectroscopy and quartz-crystal microbalance with dissipation monitoring to access the real-time kinetics and elementary solubilization steps of sub-micron sized vesicles, which are inaccessible by conventional diffraction-limited optical methods. Real-time injection of a non-ionic detergent, Triton X, induced biphasic solubilization kinetics of surface-immobilized vesicles labelled with the Dil/DiD FRET pair. The nanoscale sensitivity accessible by svFRET allowed us to unambiguously assign each kinetic step to distortions of the vesicle structure comprising an initial fast vesicle-swelling event followed by slow lipid loss and micellization. We expect the svFRET platform to be applicable beyond the sub-micron sizes studied here and become a unique tool to unravel the complex kinetics of detergent-lipid interactions.

Dynamics of intracellular neonatal Fc receptor-ligand interactions in primary macrophages using biophysical fluorescence techniques

2021 ◽  
Author(s):  
Andreas Pannek ◽  
Fiona J. Houghton ◽  
Anne M. Verhagen ◽  
Steven K. Dower ◽  
Elizabeth Hinde ◽  
...  
Keyword(s):  
Fluorescent Microscopy ◽  
High Mobility ◽  
Resonance Energy ◽  
Fc Receptor ◽  
Correlation Spectroscopy ◽  
Image Correlation ◽  
Fluorescence Lifetime Imaging ◽  
Neonatal Fc Receptor ◽  
Ligand Interactions ◽  
Kinetics Of

The neonatal Fc receptor (FcRn) is responsible for the recycling of endocytosed albumin and IgG and contributes to their long plasma half-life. We recently identified a FcRn-dependent, recycling pathway from macropinosomes in macrophages (Toh et al, 2019), however, little is known about the dynamics of intracellular FcRn-ligand interactions to promote recycling. Here we demonstrate a multiplexed biophysical fluorescent microscopy approach to resolve the spatiotemporal dynamics of albumin-FcRn interactions in living bone marrow-derived macrophages (BMDMs). We used the phasor approach to fluorescence lifetime imaging microscopy (FLIM) of Förster resonance energy transfer (FRET) to detect the interaction of a FcRn-mCherry fusion protein with endocytosed Alexa Fluor 488-labelled human serum albumin (HSA-AF488) in BMDMs, and Raster Image Correlation Spectroscopy (RICS) analysis of single fluorescent-labelled albumin molecules to monitor the diffusion kinetics of internalised albumin. Our data identified a major fraction of immobile HSA-AF488 molecules in endosomal structures of human FcRn-positive mouse macrophages and an increase in FLIM- FRET following endocytosis, including detection of FRET in tubular-like structures. A non-binding mutant of albumin showed minimum FLIM-FRET and high mobility. These data reveal the kinetics of FcRn-ligand binding within endosomal structures for recruitment into transport carriers for recycling. These approaches have wide applicability for analyses of intracellular ligand-receptor interactions.

Monitoring the intracellular transformation process of surface-cleavable PLGA particles containing disulfide bonds by fluorescence resonance energy transfer

2015 ◽  
Vol 3 (45) ◽  
pp. 8865-8873 ◽  
Author(s):  
Dahai Yu ◽  
Guangyang Zou ◽  
Xiaojing Cui ◽  
Zhengwei Mao ◽  
Irina Estrela-Lopis ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Disulfide Bonds ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Transformation Process ◽  
Fluorescence Resonance ◽  
Kinetics Of ◽  
Surface Cleavage ◽  
In Cells

The FRET technique was used to quantify the surface cleavage kinetics of PLGA particles containing disulfide bonds in cells.

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