Source 1primary paper2010Journal of the American Chemical Society
Toolkit/cryogenic-temperature ENDOR spectroscopy
cryogenic-temperature ENDOR spectroscopy
Also known as: ENDOR spectroscopy
Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Cryogenic-temperature ENDOR spectroscopy is a spectroscopic assay method applied to LOV domains to interrogate the local environment of the flavin mononucleotide (FMN) cofactor. It does so by measuring temperature-dependent hyperfine couplings associated with hindered rotation of the methyl group attached at C(8) of the FMN isoalloxazine ring.
Usefulness & Problems
Why this is useful
This method is useful for probing protein–cofactor interactions in the direct vicinity of FMN within LOV domains. The cited study states that following temperature dependencies of hyperfine couplings can report on these interactions at sub-angstrom resolution.
Problem solved
It addresses the problem of resolving subtle local interactions around the FMN cofactor in LOV domains. Specifically, it provides a way to infer the immediate protein environment by analyzing temperature-dependent methyl-group rotational behavior.
Problem links
Need conditional recombination or state switching
DerivedCryogenic-temperature ENDOR spectroscopy is a spectroscopic assay method applied to LOV domains to interrogate the local environment of the FMN cofactor. It does so by analyzing temperature-dependent hyperfine couplings associated with rotation of the methyl group at C(8) of the FMN isoalloxazine ring.
Taxonomy & Function
Primary hierarchy
Technique Branch
Method: A concrete measurement method used to characterize an engineered system.
Mechanisms
electron-nuclear double resonance measurement of hyperfine couplingselectron-nuclear double resonance measurement of hyperfine couplingstemperature-dependent probing of hindered methyl-group rotationtemperature-dependent probing of hindered methyl-group rotationTechniques
Functional AssayTarget processes
recombinationImplementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationoperating role: sensor
The assay is performed under cryogenic-temperature ENDOR conditions and requires LOV domains containing an FMN cofactor. The readout relies on analyzing the temperature dependence of hyperfine couplings linked to rotation of the methyl group at C(8) of the FMN isoalloxazine ring.
The supplied evidence is limited to application in LOV domains and to information derived from the FMN C(8) methyl group. No evidence here describes throughput, sample requirements, compatibility with non-cryogenic conditions, or validation beyond the cited 2010 study.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Protein-cofactor interactions can be probed on a sub-angstrom level by following the temperature dependencies of hyperfine couplings.
it is possible to probe protein-cofactor interactions on a sub-angstrom level by following the temperature dependencies of hyperfine couplings
spatial resolution sub-angstrom level
Protein-cofactor interactions can be probed on a sub-angstrom level by following the temperature dependencies of hyperfine couplings.
it is possible to probe protein-cofactor interactions on a sub-angstrom level by following the temperature dependencies of hyperfine couplings
spatial resolution sub-angstrom level
Protein-cofactor interactions can be probed on a sub-angstrom level by following the temperature dependencies of hyperfine couplings.
it is possible to probe protein-cofactor interactions on a sub-angstrom level by following the temperature dependencies of hyperfine couplings
spatial resolution sub-angstrom level
Protein-cofactor interactions can be probed on a sub-angstrom level by following the temperature dependencies of hyperfine couplings.
it is possible to probe protein-cofactor interactions on a sub-angstrom level by following the temperature dependencies of hyperfine couplings
spatial resolution sub-angstrom level
Protein-cofactor interactions can be probed on a sub-angstrom level by following the temperature dependencies of hyperfine couplings.
it is possible to probe protein-cofactor interactions on a sub-angstrom level by following the temperature dependencies of hyperfine couplings
spatial resolution sub-angstrom level
Protein-cofactor interactions can be probed on a sub-angstrom level by following the temperature dependencies of hyperfine couplings.
it is possible to probe protein-cofactor interactions on a sub-angstrom level by following the temperature dependencies of hyperfine couplings
spatial resolution sub-angstrom level
Protein-cofactor interactions can be probed on a sub-angstrom level by following the temperature dependencies of hyperfine couplings.
it is possible to probe protein-cofactor interactions on a sub-angstrom level by following the temperature dependencies of hyperfine couplings
spatial resolution sub-angstrom level
Protein-cofactor interactions can be probed on a sub-angstrom level by following the temperature dependencies of hyperfine couplings.
it is possible to probe protein-cofactor interactions on a sub-angstrom level by following the temperature dependencies of hyperfine couplings
spatial resolution sub-angstrom level
Protein-cofactor interactions can be probed on a sub-angstrom level by following the temperature dependencies of hyperfine couplings.
it is possible to probe protein-cofactor interactions on a sub-angstrom level by following the temperature dependencies of hyperfine couplings
spatial resolution sub-angstrom level
Protein-cofactor interactions can be probed on a sub-angstrom level by following the temperature dependencies of hyperfine couplings.
it is possible to probe protein-cofactor interactions on a sub-angstrom level by following the temperature dependencies of hyperfine couplings
spatial resolution sub-angstrom level
Protein-cofactor interactions can be probed on a sub-angstrom level by following the temperature dependencies of hyperfine couplings.
it is possible to probe protein-cofactor interactions on a sub-angstrom level by following the temperature dependencies of hyperfine couplings
spatial resolution sub-angstrom level
Protein-cofactor interactions can be probed on a sub-angstrom level by following the temperature dependencies of hyperfine couplings.
it is possible to probe protein-cofactor interactions on a sub-angstrom level by following the temperature dependencies of hyperfine couplings
spatial resolution sub-angstrom level
Protein-cofactor interactions can be probed on a sub-angstrom level by following the temperature dependencies of hyperfine couplings.
it is possible to probe protein-cofactor interactions on a sub-angstrom level by following the temperature dependencies of hyperfine couplings
spatial resolution sub-angstrom level
Protein-cofactor interactions can be probed on a sub-angstrom level by following the temperature dependencies of hyperfine couplings.
it is possible to probe protein-cofactor interactions on a sub-angstrom level by following the temperature dependencies of hyperfine couplings
spatial resolution sub-angstrom level
Protein-cofactor interactions can be probed on a sub-angstrom level by following the temperature dependencies of hyperfine couplings.
it is possible to probe protein-cofactor interactions on a sub-angstrom level by following the temperature dependencies of hyperfine couplings
spatial resolution sub-angstrom level
Protein-cofactor interactions can be probed on a sub-angstrom level by following the temperature dependencies of hyperfine couplings.
it is possible to probe protein-cofactor interactions on a sub-angstrom level by following the temperature dependencies of hyperfine couplings
spatial resolution sub-angstrom level
Protein-cofactor interactions can be probed on a sub-angstrom level by following the temperature dependencies of hyperfine couplings.
it is possible to probe protein-cofactor interactions on a sub-angstrom level by following the temperature dependencies of hyperfine couplings
spatial resolution sub-angstrom level
Cryogenic-temperature ENDOR spectroscopy can be applied to LOV domains to gain information on the direct vicinity of the FMN cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN isoalloxazine ring.
we describe how cryogenic-temperature ENDOR spectroscopy can be applied to various LOV domains ... to gain information on the direct vicinity of the flavin mononucleotide (FMN) cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN's isoalloxazine ring
Cryogenic-temperature ENDOR spectroscopy can be applied to LOV domains to gain information on the direct vicinity of the FMN cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN isoalloxazine ring.
we describe how cryogenic-temperature ENDOR spectroscopy can be applied to various LOV domains ... to gain information on the direct vicinity of the flavin mononucleotide (FMN) cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN's isoalloxazine ring
Cryogenic-temperature ENDOR spectroscopy can be applied to LOV domains to gain information on the direct vicinity of the FMN cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN isoalloxazine ring.
we describe how cryogenic-temperature ENDOR spectroscopy can be applied to various LOV domains ... to gain information on the direct vicinity of the flavin mononucleotide (FMN) cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN's isoalloxazine ring
Cryogenic-temperature ENDOR spectroscopy can be applied to LOV domains to gain information on the direct vicinity of the FMN cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN isoalloxazine ring.
we describe how cryogenic-temperature ENDOR spectroscopy can be applied to various LOV domains ... to gain information on the direct vicinity of the flavin mononucleotide (FMN) cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN's isoalloxazine ring
Cryogenic-temperature ENDOR spectroscopy can be applied to LOV domains to gain information on the direct vicinity of the FMN cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN isoalloxazine ring.
we describe how cryogenic-temperature ENDOR spectroscopy can be applied to various LOV domains ... to gain information on the direct vicinity of the flavin mononucleotide (FMN) cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN's isoalloxazine ring
Cryogenic-temperature ENDOR spectroscopy can be applied to LOV domains to gain information on the direct vicinity of the FMN cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN isoalloxazine ring.
we describe how cryogenic-temperature ENDOR spectroscopy can be applied to various LOV domains ... to gain information on the direct vicinity of the flavin mononucleotide (FMN) cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN's isoalloxazine ring
Cryogenic-temperature ENDOR spectroscopy can be applied to LOV domains to gain information on the direct vicinity of the FMN cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN isoalloxazine ring.
we describe how cryogenic-temperature ENDOR spectroscopy can be applied to various LOV domains ... to gain information on the direct vicinity of the flavin mononucleotide (FMN) cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN's isoalloxazine ring
Cryogenic-temperature ENDOR spectroscopy can be applied to LOV domains to gain information on the direct vicinity of the FMN cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN isoalloxazine ring.
we describe how cryogenic-temperature ENDOR spectroscopy can be applied to various LOV domains ... to gain information on the direct vicinity of the flavin mononucleotide (FMN) cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN's isoalloxazine ring
Cryogenic-temperature ENDOR spectroscopy can be applied to LOV domains to gain information on the direct vicinity of the FMN cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN isoalloxazine ring.
we describe how cryogenic-temperature ENDOR spectroscopy can be applied to various LOV domains ... to gain information on the direct vicinity of the flavin mononucleotide (FMN) cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN's isoalloxazine ring
Cryogenic-temperature ENDOR spectroscopy can be applied to LOV domains to gain information on the direct vicinity of the FMN cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN isoalloxazine ring.
we describe how cryogenic-temperature ENDOR spectroscopy can be applied to various LOV domains ... to gain information on the direct vicinity of the flavin mononucleotide (FMN) cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN's isoalloxazine ring
Cryogenic-temperature ENDOR spectroscopy can be applied to LOV domains to gain information on the direct vicinity of the FMN cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN isoalloxazine ring.
we describe how cryogenic-temperature ENDOR spectroscopy can be applied to various LOV domains ... to gain information on the direct vicinity of the flavin mononucleotide (FMN) cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN's isoalloxazine ring
Cryogenic-temperature ENDOR spectroscopy can be applied to LOV domains to gain information on the direct vicinity of the FMN cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN isoalloxazine ring.
we describe how cryogenic-temperature ENDOR spectroscopy can be applied to various LOV domains ... to gain information on the direct vicinity of the flavin mononucleotide (FMN) cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN's isoalloxazine ring
Cryogenic-temperature ENDOR spectroscopy can be applied to LOV domains to gain information on the direct vicinity of the FMN cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN isoalloxazine ring.
we describe how cryogenic-temperature ENDOR spectroscopy can be applied to various LOV domains ... to gain information on the direct vicinity of the flavin mononucleotide (FMN) cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN's isoalloxazine ring
Cryogenic-temperature ENDOR spectroscopy can be applied to LOV domains to gain information on the direct vicinity of the FMN cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN isoalloxazine ring.
we describe how cryogenic-temperature ENDOR spectroscopy can be applied to various LOV domains ... to gain information on the direct vicinity of the flavin mononucleotide (FMN) cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN's isoalloxazine ring
Cryogenic-temperature ENDOR spectroscopy can be applied to LOV domains to gain information on the direct vicinity of the FMN cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN isoalloxazine ring.
we describe how cryogenic-temperature ENDOR spectroscopy can be applied to various LOV domains ... to gain information on the direct vicinity of the flavin mononucleotide (FMN) cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN's isoalloxazine ring
Cryogenic-temperature ENDOR spectroscopy can be applied to LOV domains to gain information on the direct vicinity of the FMN cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN isoalloxazine ring.
we describe how cryogenic-temperature ENDOR spectroscopy can be applied to various LOV domains ... to gain information on the direct vicinity of the flavin mononucleotide (FMN) cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN's isoalloxazine ring
Cryogenic-temperature ENDOR spectroscopy can be applied to LOV domains to gain information on the direct vicinity of the FMN cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN isoalloxazine ring.
we describe how cryogenic-temperature ENDOR spectroscopy can be applied to various LOV domains ... to gain information on the direct vicinity of the flavin mononucleotide (FMN) cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN's isoalloxazine ring
Approval Evidence
1 source2 linked approval claimsfirst-pass slug cryogenic-temperature-endor-spectroscopy
we describe how cryogenic-temperature ENDOR spectroscopy can be applied to various LOV domains
Source:
measurement resolutionsupports
Protein-cofactor interactions can be probed on a sub-angstrom level by following the temperature dependencies of hyperfine couplings.
it is possible to probe protein-cofactor interactions on a sub-angstrom level by following the temperature dependencies of hyperfine couplings
Source:
method applicationsupports
Cryogenic-temperature ENDOR spectroscopy can be applied to LOV domains to gain information on the direct vicinity of the FMN cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN isoalloxazine ring.
we describe how cryogenic-temperature ENDOR spectroscopy can be applied to various LOV domains ... to gain information on the direct vicinity of the flavin mononucleotide (FMN) cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN's isoalloxazine ring
Source:
Comparisons
Source-backed strengths
The reported strength of the method is sub-angstrom sensitivity to protein–cofactor interactions based on temperature-dependent hyperfine coupling measurements. It was described as applicable to various LOV domains, indicating use across more than one member of this photoreceptor domain class.
Compared with high throughput screening
cryogenic-temperature ENDOR spectroscopy and high throughput screening address a similar problem space because they share recombination.
Shared frame: same top-level item type; shared target processes: recombination
Compared with stroke transcriptomics
cryogenic-temperature ENDOR spectroscopy and stroke transcriptomics address a similar problem space because they share recombination.
Shared frame: same top-level item type; shared target processes: recombination
Compared with whole genome screening of gene knockout mutants
cryogenic-temperature ENDOR spectroscopy and whole genome screening of gene knockout mutants address a similar problem space because they share recombination.
Shared frame: same top-level item type; shared target processes: recombination
Ranked Citations
- 1.