scholarly journals Nanosecond-order long–short fluorescence lifetime switchable encryption with enlarged coding capacity

Nanophotonics ◽  
2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Teng Luo ◽  
Yihua Zhao ◽  
Ting Zhou ◽  
Junle Qu
Keyword(s):  
Information Security ◽  
Fluorescence Lifetime ◽  
Weighted Average ◽  
Exponential Fitting ◽  
Double Exponential ◽  
Coding Capacity ◽  
Average Fluorescence

Abstract The turn-off fluorescent photoswitches for information encryption are constantly being developed. However, there are no reports about time-switchable (fluorescence lifetime-switchable) encryption to overcome the limitations of tunable encoding numbers in spectrally and temporally encoded libraries. Based on the double-exponential fitting of fluorescence lifetime, we propose, a fatigue-free and highly flexible switch between the amplitude-weighted average fluorescence lifetime (τm) and the intensity-weighted average fluorescence lifetime (τi), which will realize the supermultiplexed fluorescence lifetime switchable encryption. The potentially enormous library of different fluorescent lifetime combinations would facilitate the development of information security.

DOUBLE-EXPONENTIAL FITTING FUNCTION FOR EVALUATION OF COSMIC-RAY-INDUCED NEUTRON FLUENCE RATE IN ARBITRARY LOCATIONS

2017 ◽  
Vol 177 (3) ◽  
pp. 317-323 ◽  
Author(s):  
Huailiang Li ◽  
Yigang Yang ◽  
Qibiao Wang ◽  
Xianguo Tuo ◽  
Mark Julian Henderson ◽  
...  
Keyword(s):  
Neutron Fluence ◽  
Cosmic Ray ◽  
Exponential Fitting ◽  
Fluence Rate ◽  
Neutron Fluence Rate ◽  
Double Exponential

scholarly journals Multiphoton time-domain fluorescence lifetime imaging microscopy: practical application to protein–protein interactions using global analysis

2008 ◽  
Vol 6 (suppl_1) ◽  
Author(s):  
P.R Barber ◽  
S.M Ameer-Beg ◽  
J Gilbey ◽  
L.M Carlin ◽  
M Keppler ◽  
...  
Keyword(s):  
Fluorescence Lifetime ◽  
Protein Interactions ◽  
Time Domain ◽  
Single Photon ◽  
Global Analysis ◽  
Exponential Fitting ◽  
Fluorescence Lifetime Imaging Microscopy ◽  
Fluorescence Lifetime Imaging ◽  
Protein Protein Interactions ◽  
Lifetime Imaging

Förster resonance energy transfer (FRET) detected via fluorescence lifetime imaging microscopy (FLIM) and global analysis provide a way in which protein–protein interactions may be spatially localized and quantified within biological cells. The FRET efficiency and proportion of interacting molecules have been determined using bi-exponential fitting to time-domain FLIM data from a multiphoton time-correlated single-photon counting microscope system. The analysis has been made more robust to noise and significantly faster using global fitting, allowing higher spatial resolutions and/or lower acquisition times. Data have been simulated, as well as acquired from cell experiments, and the accuracy of a modified Levenberg–Marquardt fitting technique has been explored. Multi-image global analysis has been used to follow the epidermal growth factor-induced activation of Cdc42 in a short-image-interval time-lapse FLIM/FRET experiment. Our implementation offers practical analysis and time-resolved-image manipulation, which have been targeted towards providing fast execution, robustness to low photon counts, quantitative results and amenability to automation and batch processing.

scholarly journals Changing Times: Fluorescence-lifetime Analysis of Amyloidogenic SF-IAPP Fusion Protein

2018 ◽  
Author(s):  
Olga I Antimonova ◽  
Dmitry V Lebedev ◽  
Yana A Zabrodskaya ◽  
Natalia A Grudinina ◽  
Michael M Shavlovsky ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Fluorescence Lifetime ◽  
Fluorescent Protein ◽  
Islet Amyloid ◽  
Cellular Models ◽  
Fluorescent Lifetime Imaging Microscopy ◽  
Lifetime Analysis ◽  
Changing Times ◽  
Green Fluorescent ◽  
Average Fluorescence

AbstractThe fluorescence lifetime of the superfolder green fluorescent protein (SF) and the SF protein fused with islet amyloid polypeptide (SF-IAPP) were studied in polyacrylamide gel. It was shown that the SF average fluorescence lifetime under these conditions slightly differs from that of the SF-IAPP monomer. SF-IAPP does not lose the ability to form amyloid-like fibrils; meanwhile, the average fluorescence lifetime of the fusion protein in fibrils is reduced. We propose the application of Fluorescent-lifetime Imaging Microscopy (FLIM) to the measurement of average fluorescence lifetimes of fusion proteins (amyloidogenic protein–SF) in the context of studies using cellular models of conformational diseases.

scholarly journals Recognizing Physisorption and Chemisorption in Carbon Nanotubes Gas Sensors by Double Exponential Fitting of the Response

Sensors ◽  
2016 ◽  
Vol 16 (5) ◽  
pp. 731 ◽  
Author(s):  
Andrea Calvi ◽  
Alberto Ferrari ◽  
Luca Sbuelz ◽  
Andrea Goldoni ◽  
Silvio Modesti
Keyword(s):  
Carbon Nanotubes ◽  
Gas Sensors ◽  
Exponential Fitting ◽  
Double Exponential

Factor identification and computation in the assessment of information security risks for digital libraries

2016 ◽  
Vol 51 (1) ◽  
pp. 78-94 ◽  
Author(s):  
Shuiqing Huang ◽  
Zhengbiao Han ◽  
Bo Yang ◽  
Ni Ren
Keyword(s):  
Information Security ◽  
Digital Library ◽  
Digital Libraries ◽  
Public Library ◽  
Weighted Average ◽  
Assessment Method ◽  
Security Risk ◽  
Security Risks ◽  
Assignment Method ◽  
The Status

This study proposes an objective methodology for identifying and computing the factors relevant to the assessment of information security risks for digital libraries that is also compliant with the ISO 27000 and the GB/T 20984 standards. By introducing a fuzzy comprehensive assessment method and an expert investigation method to the dimensions of assets and threats, this study proposes a model for computing the value of assets and the severity of threats. In the dimension of vulnerabilities, a vulnerability computation model based on the multi-channel weighted average method is proposed. By considering the digital library of a typical public library in China as the object of assessment, this study acquires assessment data by using a combination of a questionnaire survey, an on-site survey and vulnerability scanning. Research findings consisted of the following: (1) the digital library identified a total of 3111 information security risk items; (2) according to the assessment results attained using a combination of the factor identification and computational methodologies proposed here in conjunction with the multiplicative method specified in GB/T 20984, the high-risk (or higher risk) items accounted for 0.9% of all risky items, which is consistent with the status quo in information security risks faced by digital libraries. The analysis showed that the proposed methodology is more scientific than the currently prevailing direct value assignment method.

DX-Center in Se-Doped AlxGa1-xAs

1989 ◽  
Vol 163 ◽  
Author(s):  
Thomas R. Hanak ◽  
Assem M. Bakry ◽  
Richard K. Ahrenkiel ◽  
Michael L. Timmons
Keyword(s):  
Cross Sections ◽  
Thermal Activation ◽  
Chemical Vapor ◽  
Exponential Fitting ◽  
Organic Chemical ◽  
Defect States ◽  
Arrhenius Plots ◽  
Double Exponential ◽  
Metal Organic ◽  
Dx Center

AbstractWe report the measurement of the thermal activation energy for the DX- center in Se-doped AlxGa1-xAs grown by metal-organic chemical vapor deposition (MOCVD) for different alloy compositions (x=0.19, 0.23, 0.27, 0.31). The peaks obtained from conventional DLTS are often broad or asymmetric with shoulders on one or both sides. These phenomena often arise from two or more traps which are active in the same temperature range.The capacitive transients are recorded digitally and analyzed directly by applying a nonlinear double exponential fitting routine to the data. This fitting produces two Arrhenius plots and yields the densities of the defect states. From the Arrhenius plots, the capture cross sections at infinite temperature and the thermal activation energies are calculated. These results are then used to simulate the DLTS spectra. Excellent agreement between real and simulated spectra is shown.

scholarly journals Bioenergetic Alterations of Metabolic Redox Coenzymes as NADH, FAD and FMN by Means of Fluorescence Lifetime Imaging Techniques

2021 ◽  
Vol 22 (11) ◽  
pp. 5952
Author(s):  
Sviatlana Kalinina ◽  
Christian Freymueller ◽  
Nilanjon Naskar ◽  
Bjoern von Einem ◽  
Kirsten Reess ◽  
...  
Keyword(s):  
Fluorescence Lifetime ◽  
Imaging Techniques ◽  
Cell Metabolism ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Flavin Mononucleotide ◽  
Exponential Fitting ◽  
Fluorescence Lifetime Imaging ◽  
Lifetime Imaging ◽  
Significant Difference ◽  
Redox Coenzymes

Metabolic FLIM (fluorescence lifetime imaging) is used to image bioenergetic status in cells and tissue. Whereas an attribution of the fluorescence lifetime of coenzymes as an indicator for cell metabolism is mainly accepted, it is debated whether this is valid for the redox state of cells. In this regard, an innovative algorithm using the lifetime characteristics of nicotinamide adenine dinucleotide (phosphate) (NAD(P)H) and flavin adenine dinucleotide (FAD) to calculate the fluorescence lifetime induced redox ratio (FLIRR) has been reported so far. We extended the FLIRR approach and present new results, which includes FLIM data of the various enzymes, such as NAD(P)H, FAD, as well as flavin mononucleotide (FMN). Our algorithm uses a two-exponential fitting procedure for the NAD(P)H autofluorescence and a three-exponential fit of the flavin signal. By extending the FLIRR approach, we introduced FLIRR1 as protein-bound NAD(P)H related to protein-bound FAD, FLIRR2 as protein-bound NAD(P)H related to free (unbound) FAD and FLIRR3 as protein-bound NAD(P)H related to protein-bound FMN. We compared the significance of extended FLIRR to the metabolic index, defined as the ratio of protein-bound NAD(P)H to free NAD(P)H. The statistically significant difference for tumor and normal cells was found to be highest for FLIRR1.

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