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Search Results (3)

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Keywords = pulsed interleaved excitation

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14 pages, 4850 KB  
Article
Design and Implementation of a Low-Power Low-Cost Digital Current-Sink Electronic Load ‡
by Wei Jiang, Jieyun Wang, Qianlong Wang, Song Xu, Seiji Hashimoto and Zhong Liu
Energies 2019, 12(13), 2611; https://doi.org/10.3390/en12132611 - 7 Jul 2019
Cited by 4 | Viewed by 4645
Abstract
Electronic load (e-load) is essential equipment for power converter performance test, where a designated load profile is executed. Electronic load is usually implemented with the analog controller for fast tracking of the load profile reference. In this paper, a low-power low-cost electronic load [...] Read more.
Electronic load (e-load) is essential equipment for power converter performance test, where a designated load profile is executed. Electronic load is usually implemented with the analog controller for fast tracking of the load profile reference. In this paper, a low-power low-cost electronic load is proposed. MOSFETs (metal-oxide-semiconductor field-effect transistors) are used as the power consumption devices, which are regulated to the active region as controlled current-sink. In order to achieve fast transient response using the low-cost digital signal controller (DSC) PWM peripherals, the interleaving PWM method is proposed to achieve active current ripple mitigation. To obtain the system open-loop gain for current-sink operation, an offline digital system identification method, followed by model reduction, is proposed by applying Pseudo-Random Binary Sequence (PRBS) excitation. Pole-zero cancelation method is used in the control system design and later implemented in a DSC. The prototype is built and tested, in which meaningful testing scenarios under constant current-sink mode, pulse current sink mode, and double line-frequency current mode are verified. The experimental results indicate that the proposed e-load can sink pre-programmed current profile with well-attenuated ripple for static and dynamic load testing, and is applicable to fully digitalized power testing equipment. Full article
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23 pages, 1981 KB  
Article
Inter-Dye Distance Distributions Studied by a Combination of Single-Molecule FRET-Filtered Lifetime Measurements and a Weighted Accessible Volume (wAV) Algorithm
by Henning Höfig, Matteo Gabba, Simón Poblete, Daryan Kempe and Jörg Fitter
Molecules 2014, 19(12), 19269-19291; https://doi.org/10.3390/molecules191219269 - 25 Nov 2014
Cited by 30 | Viewed by 9498
Abstract
Förster resonance energy transfer (FRET) is an important tool for studying the structural and dynamical properties of biomolecules. The fact that both the internal dynamics of the biomolecule and the movements of the biomolecule-attached dyes can occur on similar timescales of nanoseconds is [...] Read more.
Förster resonance energy transfer (FRET) is an important tool for studying the structural and dynamical properties of biomolecules. The fact that both the internal dynamics of the biomolecule and the movements of the biomolecule-attached dyes can occur on similar timescales of nanoseconds is an inherent problem in FRET studies. By performing single-molecule FRET-filtered lifetime measurements, we are able to characterize the amplitude of the motions of fluorescent probes attached to double-stranded DNA standards by means of flexible linkers. With respect to previously proposed experimental approaches, we improved the precision and the accuracy of the inter-dye distance distribution parameters by filtering out the donor-only population with pulsed interleaved excitation. A coarse-grained model is employed to reproduce the experimentally determined inter-dye distance distributions. This approach can easily be extended to intrinsically flexible proteins allowing, under certain conditions, to decouple the macromolecule amplitude of motions from the contribution of the dye linkers. Full article
(This article belongs to the Special Issue Single Molecule Techniques)
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19 pages, 1372 KB  
Article
Early Amyloidogenic Oligomerization Studied through Fluorescence Lifetime Correlation Spectroscopy
by Jose M. Paredes, Salvador Casares, Maria J. Ruedas-Rama, Elena Fernandez, Fabio Castello, Lorena Varela and Angel Orte
Int. J. Mol. Sci. 2012, 13(8), 9400-9418; https://doi.org/10.3390/ijms13089400 - 25 Jul 2012
Cited by 24 | Viewed by 8298
Abstract
Amyloidogenic protein aggregation is a persistent biomedical problem. Despite active research in disease-related aggregation, the need for multidisciplinary approaches to the problem is evident. Recent advances in single-molecule fluorescence spectroscopy are valuable for examining heterogenic biomolecular systems. In this work, we have explored [...] Read more.
Amyloidogenic protein aggregation is a persistent biomedical problem. Despite active research in disease-related aggregation, the need for multidisciplinary approaches to the problem is evident. Recent advances in single-molecule fluorescence spectroscopy are valuable for examining heterogenic biomolecular systems. In this work, we have explored the initial stages of amyloidogenic aggregation by employing fluorescence lifetime correlation spectroscopy (FLCS), an advanced modification of conventional fluorescence correlation spectroscopy (FCS) that utilizes time-resolved information. FLCS provides size distributions and kinetics for the oligomer growth of the SH3 domain of α-spectrin, whose N47A mutant forms amyloid fibrils at pH 3.2 and 37 °C in the presence of salt. The combination of FCS with additional fluorescence lifetime information provides an exciting approach to focus on the initial aggregation stages, allowing a better understanding of the fibrillization process, by providing multidimensional information, valuable in combination with other conventional methodologies. Full article
(This article belongs to the Special Issue Advances in Single Molecule Spectroscopy)
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