Deconvolution of fluorescence decay curves.  A critical comparison of techniques

O’Connor, Desmond; Ware, William R.; André, Jean‐Claude

doi:10.1021/j100473a019

Cited by 328 publications

(137 citation statements)

References 8 publications

Supporting

Mentioning

132

Contrasting

Order By: Relevance

“…We have measured the temporal decay of several samples at cryogenic and room temperature over a broad range of detection energies comprising the QW ground-state transition and the CHC luminescence. All decays are mono-exponential 23 and the corresponding decay times that result from a deconvolution with the instrument response function 24 are plotted in Fig. 4 (red squares) as a function of detection energy.…”

Section: Figmentioning

confidence: 99%

Polarization-induced confinement of continuous hole-states in highly pumped, industrial-grade, green InGaN quantum wells

Nippert

Nirschl

Schulz

et al. 2016

Journal of Applied Physics

View full text Add to dashboard Cite

We investigate industrial-grade InGaN/GaN quantum wells (QWs) emitting in the green spectral region under high, resonant pumping conditions. Consequently, an ubiquitous high energy luminescence is observed that we assign to a polarization field Confined Hole Continuum (CHC). Our finding is supported by a unique combination of experimental techniques, including transmission electron microscopy, (time-resolved) photoluminescence under various excitation conditions, and electroluminescence, which confirm an extended out-of-plane localization of the CHC-states. The larger width of this localization volume surpasses the QW thickness, yielding enhanced nonradiative losses due to point defects and interfaces, whereas the energetic proximity to the bulk valence band states promotes carrier leakage. Published by AIP Publishing.

show abstract

Section: Figmentioning

confidence: 99%

Polarization-induced confinement of continuous hole-states in highly pumped, industrial-grade, green InGaN quantum wells

Nippert

Nirschl

Schulz

et al. 2016

Journal of Applied Physics

View full text Add to dashboard Cite

show abstract

“…In this latter case, the small curvature in the SternVolmer plot would probably be caused by the occurrence of multiple conformations in solution. Furthermore, the influence of aspartic residues in close proximity to tryptophan 79 within the 5-167 actin fragment must also be taken into account (47). The CD spectrum shown in Fig.…”

Section: Involvement Of Actin Subdomain 1 In the Interaction Withmentioning

confidence: 99%

The Identification of a Second Cofilin Binding Site on Actin Suggests a Novel, Intercalated Arrangement of F-actin Binding

Renoult

Ternent²,

Maciver³

et al. 1999

Journal of Biological Chemistry

View full text Add to dashboard Cite

The cofilins are members of a protein family that binds monomeric and filamentous actin, severs actin filaments, and increases monomer off-rate from the pointed end. Here, we characterize the cofilin-actin interface. We confirm earlier work suggesting the importance of the lower region of subdomain 1 encompassing the N and C termini (site 1) in cofilin binding. In addition, we report the discovery of a new cofilin binding site (site 2) from residues 112-125 that form a helix toward the upper, rear surface of subdomain 1 in the standard actin orientation (Kabsch, W., Mannherz, H. G., Suck, D., Pai, E. F., and Holmes, K. C. (1990) Nature 347, 37-44). We propose that cofilin binds "behind" one monomer and "in front" of the other longitudinally associated monomer, accounting for the fact that cofilin alters the twist in the actin (McGough, A., Pope, B., Chiu, W., and Weeds, A. (1997) J. Cell Biol. 138, 771-781). The characterization of the cofilin-actin interface will facilitate an understanding of how cofilin severs and depolymerizes filaments and may shed light on the mechanism of the gelsolin family because they share a similar fold with the cofilins (Hatanaka, H., Ogura, K., Moriyama, K., Ichikawa, S., Yahara, I., and Inagiki, F. (1996) Cell 85, 1047-1055).Many motile processes in cells require cyclic polymerization and depolymerization of actin filaments. In cell locomotion for example, actin is polymerized at the leading edge of the cell and is recycled by depolymerizing toward the cell center. The rate constants of pure actin have been established (1), and it is clear that a discrepancy exists between these known rates and those calculated from filament turnover in cells (2). A host of actinbinding proteins are known that dramatically alter the behavior of actin in vitro, and of these, the cofilins have been suggested to have the correct properties to increase filament turnover in cells (3). This view has been confirmed by studies with living Saccharomyces (4) and Dictyostelium (5) and by Listeria motility assays (6, 7).The cofilins are a group of low molecular mass (15-21 kDa), actin-binding proteins that depolymerize actin filaments (8).This group includes vertebrate cofilin (9) and ADF 1 (10), twinstar from Drosophila (11), depactin from echinoderms (12), ADFs from plants (13), Unc-60 from nematode (14), cofilins from Saccharomyces (15, 16) and Dictyostelium (17), and actophorin from Acanthamoeba castellanii (18).The mechanism by which cofilin depolymerizes actin filament has been contentious. Soon after the discovery of the first member of the family (10), several authors suggested that depolymerization occurred through severing (9, 18). Evidence for a severing mechanism later came from videomicroscopy (19,20), but this was later challenged (6) as it was shown (6, 21) that cofilins increased the off-rate from the pointed end of the filament. However, the two opinions are not necessarily exclusive (22-24), and a similar mechanism has been proposed for both events (23). We report the identification of a cof...

show abstract

“…All the parameters in equation 2 and the time difference between the experimental and simulated fluorescence decay curves, ∆t, were determined using a nonlinear, least-squares iterative convolution method based on the Marquardt algorithm [8,9]. Scattered light of a laser pulse is used as L(t).…”

Section: Methodsmentioning

confidence: 99%

Fluorescent Nanoparticles of 2-Ethylanthracene and Pyrene

Kasatani

Masaki

Morita

et al. 2013

Trans. Mat. Res. Soc. Japan

View full text Add to dashboard Cite

Fluorescence behavior of nanoparticles of two aromatic compounds, 2-ethylanthracene and pyrene, was studied. Doped nanoparticles were also studied. Transparent organic nanoparticles dispersed in water were prepared by reprecipitation method. Polyvinyl alcohol was added in water to improve stability of organic nanoparticles. Fluorescence spectra and fluorescence quantum yields were measured by an absolute photoluminescence quantum yield measurement system. Fluorescence lifetimes were measured with a combination of a femtosecond Ti:sapphire laser and a streak camera. Fluorescence behavior of 2-ethylanthracene nanoparticles doped with naphthacene, pyrene nanoparticles doped with perylene, and polycrystals of 2-ethylanthracene and pyrene, was measured. Doping of nanoparticles with dopant quenched fluorescence of nanoparticles and strong fluorescence of dopant was observed. Fluorescence quantum yield of 2-ethylnaphthacene nanoparticles doped with naphthacene and that of pyrene nanoparticles doped with perylene were as high as 0.52 and 0.58, respectively.

show abstract

Deconvolution of fluorescence decay curves. A critical comparison of techniques

Abstract: 13) Note the value reported in ref 14 was not corrected for the error reported by Allendoerfer (ref 15). All other g values reported therein were so corrected.

Cited by 328 publications

References 8 publications

Polarization-induced confinement of continuous hole-states in highly pumped, industrial-grade, green InGaN quantum wells

Polarization-induced confinement of continuous hole-states in highly pumped, industrial-grade, green InGaN quantum wells

The Identification of a Second Cofilin Binding Site on Actin Suggests a Novel, Intercalated Arrangement of F-actin Binding

Fluorescent Nanoparticles of 2-Ethylanthracene and Pyrene

Contact Info

Product

Resources

About