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Lifetime of Fluorescence

"Lifetime of Fluorescence"에 대한 내용입니다. 굉장히 상세한 내용과 post-lab question까지 포함되어 있습니다.
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최초등록일 2024.11.15 최종저작일 2023.10
형광 만점 Quenching lifetime
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Lifetime of Fluorescence
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    소개

    "Lifetime of Fluorescence"에 대한 내용입니다.

    굉장히 상세한 내용과 post-lab question까지 포함되어 있습니다.

    목차

    1. Background
    2. Results
    3. Discussion
    4. Post-lab questions

    본문내용

    1. Background
    Luminescence is observed as a direct consequence of electrons being excited and relaxed to the ground state. After being excited to a higher energy level, electrons can undergo various pathways. For an electron in the S0 state, initial excitement using laser can make it go to the S1 state or higher. Electrons that are excited to higher vibrational state are quickly relaxed to the lowest vibrational level of S1, also known as internal conversion. Here, the electron can directly relax into S0 state, which results in fluorescence, or it may first undergo intersystem crossing to the triple state and then phosphoresce to S0 state. Such change of energy and spin state of electrons can be depicted using a Jablonski diagram.

    <중 략>

    In this experiment, we aim to measure fluorescence lifetime of coumarin, riboflavin and flavin adenine dinucleotide (FAD). Coumarin was prepared with ethanol as solvent, and riboflavin and FAD were prepared as aqueous solutions. The pH for riboflavin solution was arranged as 1, 4, 7, 10 and 13, while the pH of FAD solution was 7. The solutions were excited using diode laser at 375 nm, and the intensity was measured using TCSPC.

    참고자료

    · Lakowicz, J.R., Principles of fluorescence spectroscopy. 2nd ed. 1999, New York: Kluwer Academic/Plenum. xxiii, 698 p.
    · Becker, W., Introduction to Multi-dimensional TCSPC. 2015, Springer International Publishing. p. 1-63.
    · Jones, G., W.R. Jackson, and A.M. Halpern, Medium Effects on Fluorescence Quantum Yields and Lifetimes for Coumarin Laser-Dyes. Chemical Physics Letters, 1980. 72(2): p. 391-395.
    · Drössler, P., et al., pH dependence of the absorption and emission behaviour of riboflavin in aqueous solution. Chemical Physics, 2002. 282(3): p. 429-439.
    · Islam, S.D.M., et al., Fluorescence quenching of flavin adenine dinucleotide in aqueous solution by pH dependent isomerisation and photo-induced electron transfer. Chemical Physics, 2003. 295(2): p. 137-149.

  • AI와 토픽 톺아보기

    • 1. Fluorescence Lifetime
      Fluorescence lifetime is a fundamental property of fluorescent molecules that describes the average time a fluorophore remains in the excited state before returning to the ground state by emitting a photon. This parameter provides valuable information about the local environment and dynamics of the fluorescent species, which is crucial in various fields such as biochemistry, biophysics, and materials science. Understanding fluorescence lifetime is essential for techniques like Förster Resonance Energy Transfer (FRET), which relies on the distance-dependent energy transfer between donor and acceptor fluorophores. Measuring and analyzing fluorescence lifetimes can reveal insights into molecular interactions, conformational changes, and the presence of quenchers or other environmental factors that influence the excited-state dynamics of the fluorescent probes. The development of advanced time-resolved fluorescence techniques, such as Time-Correlated Single Photon Counting (TCSPC), has significantly improved the precision and sensitivity of fluorescence lifetime measurements, enabling their widespread application in diverse research areas.
    • 2. Time-Correlated Single Photon Counting (TCSPC)
      Time-Correlated Single Photon Counting (TCSPC) is a powerful technique for measuring fluorescence lifetimes with high temporal resolution and sensitivity. TCSPC relies on the detection of individual photons emitted by fluorescent molecules and the precise measurement of the time delay between the excitation pulse and the emission of each photon. By accumulating a large number of these time-resolved photon events, a histogram is generated that represents the fluorescence decay curve. This approach allows for the accurate determination of fluorescence lifetimes, even in the presence of complex multi-exponential decays. TCSPC has become a widely adopted method in various fields, including biology, materials science, and photophysics, due to its ability to provide detailed information about the excited-state dynamics of fluorescent species. The continuous advancements in TCSPC instrumentation, such as the development of more efficient detectors and advanced data analysis algorithms, have further expanded the capabilities of this technique, enabling the study of complex systems and the exploration of new applications in fluorescence-based research.
    • 3. Fluorescence Quenching
      Fluorescence quenching is a process in which the fluorescence intensity of a fluorophore is reduced or completely suppressed due to various mechanisms. This phenomenon can occur through different pathways, such as dynamic quenching, where the fluorophore interacts with a quencher molecule in the excited state, or static quenching, where the fluorophore and quencher form a non-fluorescent complex. Fluorescence quenching can provide valuable insights into the local environment and interactions of fluorescent species, and it has numerous applications in various fields. For example, in biochemistry and biophysics, fluorescence quenching is used to study protein-ligand interactions, conformational changes, and the accessibility of fluorescent probes to quenchers. In materials science, fluorescence quenching is employed to investigate energy transfer processes, charge transfer dynamics, and the presence of defects or impurities in materials. Understanding the mechanisms and kinetics of fluorescence quenching is crucial for the design and optimization of fluorescence-based sensors, probes, and imaging techniques, as well as for the development of new materials with tailored photophysical properties.
    • 4. Coumarin Fluorescence Lifetime
      Coumarin is a class of organic compounds that exhibit fluorescence properties, making them useful as fluorescent probes and dyes in various applications. The fluorescence lifetime of coumarin derivatives is an important parameter that provides insights into the excited-state dynamics and local environment of these fluorophores. Coumarin fluorescence lifetimes can be influenced by factors such as solvent polarity, pH, temperature, and the presence of quenchers or other interacting species. Measuring the fluorescence lifetime of coumarin compounds can reveal information about their interactions with biomolecules, the rigidity of their local environment, and the accessibility of the fluorophore to quenchers. This knowledge is valuable in fields like biochemistry, biophysics, and materials science, where coumarin-based fluorescent probes are widely used for applications such as sensing, imaging, and energy transfer studies. Understanding the factors that govern the fluorescence lifetime of coumarin derivatives is crucial for the rational design and optimization of these fluorescent probes to enhance their sensitivity, specificity, and performance in diverse research and technological applications.
    • 5. Riboflavin Fluorescence Lifetime
      Riboflavin, also known as vitamin B2, is a naturally occurring fluorescent compound that plays a crucial role in various biological processes. The fluorescence lifetime of riboflavin is an important parameter that can provide insights into its local environment and interactions within biological systems. Riboflavin exhibits a characteristic fluorescence emission that is sensitive to factors such as pH, temperature, and the presence of other biomolecules or quenchers. Measuring the fluorescence lifetime of riboflavin can reveal information about its binding interactions with proteins, its accessibility to quenchers, and its conformational changes in different cellular or physiological contexts. This knowledge is valuable in fields like biochemistry, nutrition, and biomedical research, where riboflavin is used as a fluorescent marker, a redox-active cofactor, and a potential therapeutic agent. Understanding the factors that influence the fluorescence lifetime of riboflavin can aid in the development of more sensitive and specific fluorescence-based techniques for the detection, quantification, and monitoring of this essential nutrient in biological systems, as well as in the design of riboflavin-based fluorescent probes and sensors for various applications.
    • 6. FAD Fluorescence Lifetime
      Flavin adenine dinucleotide (FAD) is a cofactor that plays a crucial role in numerous enzymatic reactions and cellular processes. FAD exhibits intrinsic fluorescence, and the measurement of its fluorescence lifetime can provide valuable insights into its local environment and interactions within biological systems. The fluorescence lifetime of FAD is sensitive to factors such as the redox state, binding interactions with proteins, and the presence of quenchers or other biomolecules. Analyzing the fluorescence lifetime of FAD can reveal information about the conformational changes, accessibility, and dynamics of this cofactor in various cellular contexts. This knowledge is particularly important in fields like biochemistry, biophysics, and biomedical research, where FAD-dependent enzymes and processes are extensively studied. Understanding the factors that influence the fluorescence lifetime of FAD can aid in the development of more sensitive and specific fluorescence-based techniques for the detection, quantification, and monitoring of this essential cofactor in biological systems. Additionally, the fluorescence lifetime of FAD can be used as a probe to study the activity and regulation of FAD-dependent enzymes, as well as to investigate the role of FAD in cellular metabolism and signaling pathways.

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