Source 1primary paper2008Physical Chemistry Chemical Physics
Toolkit/fluorescence line narrowing
fluorescence line narrowing
Also known as: FLN
Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Fluorescence line narrowing (FLN) is a spectroscopic assay method used in the cited study to interrogate the electronic structure of flavin mononucleotide (FMN) within phototropin LOV2 domains. In this context, FLN was applied to support mechanistic analysis of how the conserved cysteine near FMN perturbs the chromophore ground state and promotes photochemistry.
Usefulness & Problems
Why this is useful
FLN is useful for resolving chromophore electronic-state features that are not captured by less selective fluorescence measurements. In the cited LOV2 study, it was used to examine FMN in its protein environment and support interpretation of enhanced intersystem crossing and cysteine-enabled photochemical reactivity.
Source:
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
Problem solved
This method helps address the problem of determining how the local protein environment, specifically the conserved LOV2 cysteine, alters FMN electronic structure and photochemical behavior. The supplied evidence links this question to rapid formation of the reactive FMN triplet state and subsequent FMN-cysteine adduct formation.
Taxonomy & Function
Primary hierarchy
Technique Branch
Method: A concrete measurement method used to characterize an engineered system.
Mechanisms
electronic-state resolutionelectronic-state resolutionfluorescence spectroscopyfluorescence spectroscopyTechniques
Functional AssayTarget processes
No target processes tagged yet.
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationoperating role: sensor
The documented implementation is in a study of flavin mononucleotide in phototropin LOV2 domains, with emphasis on the conserved cysteine C450 positioned near FMN. The provided evidence does not specify instrumentation, excitation conditions, sample preparation, temperature, or construct design details.
The supplied evidence only states that FLN was applied and does not provide experimental parameters, spectral resolution metrics, or comparative benchmarking against other spectroscopic methods. Validation is limited to a single cited study context involving FMN in phototropin LOV2 domains.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
AsLOV2-C450A shows small but significant vibrational spectral shifts relative to wild-type AsLOV2 and Phy3LOV2, including down-shift of Ring I vibrations, upshifts of Ring II and III vibrations, and an upshift of the C2=O mode.
The vibrational spectrum of AsLOV2-C450A showed small but significant shifts with respect to those of wild type AsLOV2 and Phy3LOV2, with a systematic down-shift of Ring I vibrations, upshifts of Ring II and III vibrations and an upshift of the C2=O mode.
AsLOV2-C450A shows small but significant vibrational spectral shifts relative to wild-type AsLOV2 and Phy3LOV2, including down-shift of Ring I vibrations, upshifts of Ring II and III vibrations, and an upshift of the C2=O mode.
The vibrational spectrum of AsLOV2-C450A showed small but significant shifts with respect to those of wild type AsLOV2 and Phy3LOV2, with a systematic down-shift of Ring I vibrations, upshifts of Ring II and III vibrations and an upshift of the C2=O mode.
AsLOV2-C450A shows small but significant vibrational spectral shifts relative to wild-type AsLOV2 and Phy3LOV2, including down-shift of Ring I vibrations, upshifts of Ring II and III vibrations, and an upshift of the C2=O mode.
The vibrational spectrum of AsLOV2-C450A showed small but significant shifts with respect to those of wild type AsLOV2 and Phy3LOV2, with a systematic down-shift of Ring I vibrations, upshifts of Ring II and III vibrations and an upshift of the C2=O mode.
AsLOV2-C450A shows small but significant vibrational spectral shifts relative to wild-type AsLOV2 and Phy3LOV2, including down-shift of Ring I vibrations, upshifts of Ring II and III vibrations, and an upshift of the C2=O mode.
The vibrational spectrum of AsLOV2-C450A showed small but significant shifts with respect to those of wild type AsLOV2 and Phy3LOV2, with a systematic down-shift of Ring I vibrations, upshifts of Ring II and III vibrations and an upshift of the C2=O mode.
AsLOV2-C450A shows small but significant vibrational spectral shifts relative to wild-type AsLOV2 and Phy3LOV2, including down-shift of Ring I vibrations, upshifts of Ring II and III vibrations, and an upshift of the C2=O mode.
The vibrational spectrum of AsLOV2-C450A showed small but significant shifts with respect to those of wild type AsLOV2 and Phy3LOV2, with a systematic down-shift of Ring I vibrations, upshifts of Ring II and III vibrations and an upshift of the C2=O mode.
AsLOV2-C450A shows small but significant vibrational spectral shifts relative to wild-type AsLOV2 and Phy3LOV2, including down-shift of Ring I vibrations, upshifts of Ring II and III vibrations, and an upshift of the C2=O mode.
The vibrational spectrum of AsLOV2-C450A showed small but significant shifts with respect to those of wild type AsLOV2 and Phy3LOV2, with a systematic down-shift of Ring I vibrations, upshifts of Ring II and III vibrations and an upshift of the C2=O mode.
AsLOV2-C450A shows small but significant vibrational spectral shifts relative to wild-type AsLOV2 and Phy3LOV2, including down-shift of Ring I vibrations, upshifts of Ring II and III vibrations, and an upshift of the C2=O mode.
The vibrational spectrum of AsLOV2-C450A showed small but significant shifts with respect to those of wild type AsLOV2 and Phy3LOV2, with a systematic down-shift of Ring I vibrations, upshifts of Ring II and III vibrations and an upshift of the C2=O mode.
AsLOV2-C450A shows small but significant vibrational spectral shifts relative to wild-type AsLOV2 and Phy3LOV2, including down-shift of Ring I vibrations, upshifts of Ring II and III vibrations, and an upshift of the C2=O mode.
The vibrational spectrum of AsLOV2-C450A showed small but significant shifts with respect to those of wild type AsLOV2 and Phy3LOV2, with a systematic down-shift of Ring I vibrations, upshifts of Ring II and III vibrations and an upshift of the C2=O mode.
AsLOV2-C450A shows small but significant vibrational spectral shifts relative to wild-type AsLOV2 and Phy3LOV2, including down-shift of Ring I vibrations, upshifts of Ring II and III vibrations, and an upshift of the C2=O mode.
The vibrational spectrum of AsLOV2-C450A showed small but significant shifts with respect to those of wild type AsLOV2 and Phy3LOV2, with a systematic down-shift of Ring I vibrations, upshifts of Ring II and III vibrations and an upshift of the C2=O mode.
AsLOV2-C450A shows small but significant vibrational spectral shifts relative to wild-type AsLOV2 and Phy3LOV2, including down-shift of Ring I vibrations, upshifts of Ring II and III vibrations, and an upshift of the C2=O mode.
The vibrational spectrum of AsLOV2-C450A showed small but significant shifts with respect to those of wild type AsLOV2 and Phy3LOV2, with a systematic down-shift of Ring I vibrations, upshifts of Ring II and III vibrations and an upshift of the C2=O mode.
Approval Evidence
1 source1 linked approval claimfirst-pass slug fluorescence-line-narrowing
we applied fluorescence line narrowing (FLN)
Source:
method performancesupports
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Source:
Comparisons
Source-backed strengths
The cited application shows that FLN can be used as a mechanistic spectroscopy tool for FMN embedded in LOV2 domains rather than only for flavin in solution. Its value here is its ability to support analysis of electronic-state perturbation associated with enhanced intersystem crossing and cysteine-dependent photochemistry.
Source:
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
Compared with Field-domain rapid-scan EPR at 240 GHz
fluorescence line narrowing and Field-domain rapid-scan EPR at 240 GHz address a similar problem space.
Shared frame: same top-level item type
Compared with high throughput screening
fluorescence line narrowing and high throughput screening address a similar problem space.
Shared frame: same top-level item type
Compared with native green gel system
fluorescence line narrowing and native green gel system address a similar problem space.
Shared frame: same top-level item type
Strengths here: looks easier to implement in practice.
Ranked Citations
- 1.