Source 1primary paper2017Scientific Reports
Toolkit/electron-electron double resonance spectroscopy
electron-electron double resonance spectroscopy
Also known as: ELDOR spectroscopy, electron-electron double resonance (ELDOR) spectroscopy
Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Electron-electron double resonance (ELDOR) spectroscopy is a structural assay method that, when combined with site-directed spin labelling, was used to chart light-induced structural transitions in the engineered LOV histidine kinase YF1. In the cited study, it provided pairwise distance information used to model blue-light-driven quaternary rearrangements in a signaling photoreceptor.
Usefulness & Problems
Why this is useful
This method is useful for resolving light-dependent structural changes in proteins that are difficult to infer from sequence or endpoint functional readouts alone. The cited work indicates that ELDOR-based distance constraints can provide mechanistic insight into signal trajectories of LOV photoreceptors and histidine kinases and inform molecular simulations and receptor engineering.
Problem solved
It addresses the problem of experimentally charting blue-light-induced conformational and quaternary transitions in signaling proteins such as YF1. Specifically, it enables extraction of pairwise distance constraints from spin-labelled sites to support structural modelling of signal propagation.
Problem links
Need conditional control of signaling activity
DerivedElectron-electron double resonance (ELDOR) spectroscopy, used with site-directed spin labelling, is an assay method for charting light-induced structural transitions in proteins. In the cited work, it was applied to the engineered LOV histidine kinase YF1 to derive pair-wise distance constraints and model blue-light-driven quaternary rearrangements.
Need precise spatiotemporal control with light input
DerivedElectron-electron double resonance (ELDOR) spectroscopy, used with site-directed spin labelling, is an assay method for charting light-induced structural transitions in proteins. In the cited work, it was applied to the engineered LOV histidine kinase YF1 to derive pair-wise distance constraints and model blue-light-driven quaternary rearrangements.
Taxonomy & Function
Primary hierarchy
Technique Branch
Method: A concrete measurement method used to characterize an engineered system.
Mechanisms
Heterodimerizationlight-induced conformational switchinglight-induced conformational switchingquaternary structural rearrangementquaternary structural rearrangementrotation and splaying of dimeric photosensor unitsrotation and splaying of dimeric photosensor unitsTarget processes
signalingInput: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: multi component delivery burdenimplementation constraint: spectral hardware requirementoperating role: sensorswitch architecture: multi componentswitch architecture: recruitment
The documented implementation combines ELDOR spectroscopy with site-directed spin labelling, implying the need for labelled protein constructs at defined positions. The evidence does not provide further procedural details such as spin label chemistry, expression system, buffer conditions, or illumination protocol beyond blue-light stimulation.
The supplied evidence supports use in a specific engineered LOV histidine kinase context and does not establish broad performance across diverse proteins or conditions. Practical details such as distance range, temporal resolution, sample requirements, and comparative benchmarking against other structural methods are not provided in the evidence.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
A photoreceptor variant with an inverted signal response has a drastically altered dimer interface but shows linker structural transitions similar to those in YF1 under light stimulation.
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
A photoreceptor variant with an inverted signal response has a drastically altered dimer interface but shows linker structural transitions similar to those in YF1 under light stimulation.
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
A photoreceptor variant with an inverted signal response has a drastically altered dimer interface but shows linker structural transitions similar to those in YF1 under light stimulation.
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
A photoreceptor variant with an inverted signal response has a drastically altered dimer interface but shows linker structural transitions similar to those in YF1 under light stimulation.
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
A photoreceptor variant with an inverted signal response has a drastically altered dimer interface but shows linker structural transitions similar to those in YF1 under light stimulation.
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
A photoreceptor variant with an inverted signal response has a drastically altered dimer interface but shows linker structural transitions similar to those in YF1 under light stimulation.
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
A photoreceptor variant with an inverted signal response has a drastically altered dimer interface but shows linker structural transitions similar to those in YF1 under light stimulation.
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
A photoreceptor variant with an inverted signal response has a drastically altered dimer interface but shows linker structural transitions similar to those in YF1 under light stimulation.
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
A photoreceptor variant with an inverted signal response has a drastically altered dimer interface but shows linker structural transitions similar to those in YF1 under light stimulation.
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
A photoreceptor variant with an inverted signal response has a drastically altered dimer interface but shows linker structural transitions similar to those in YF1 under light stimulation.
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
A photoreceptor variant with an inverted signal response has a drastically altered dimer interface but shows linker structural transitions similar to those in YF1 under light stimulation.
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
A photoreceptor variant with an inverted signal response has a drastically altered dimer interface but shows linker structural transitions similar to those in YF1 under light stimulation.
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
A photoreceptor variant with an inverted signal response has a drastically altered dimer interface but shows linker structural transitions similar to those in YF1 under light stimulation.
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
A photoreceptor variant with an inverted signal response has a drastically altered dimer interface but shows linker structural transitions similar to those in YF1 under light stimulation.
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
A photoreceptor variant with an inverted signal response has a drastically altered dimer interface but shows linker structural transitions similar to those in YF1 under light stimulation.
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
A photoreceptor variant with an inverted signal response has a drastically altered dimer interface but shows linker structural transitions similar to those in YF1 under light stimulation.
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
A photoreceptor variant with an inverted signal response has a drastically altered dimer interface but shows linker structural transitions similar to those in YF1 under light stimulation.
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
The study provides mechanistic insight into signal trajectories of LOV photoreceptors and histidine kinases that can inform molecular simulations and engineering of novel receptors.
Taken together, we provide mechanistic insight into the signal trajectories of LOV photoreceptors and histidine kinases that inform molecular simulations and the engineering of novel receptors.
The study provides mechanistic insight into signal trajectories of LOV photoreceptors and histidine kinases that can inform molecular simulations and engineering of novel receptors.
Taken together, we provide mechanistic insight into the signal trajectories of LOV photoreceptors and histidine kinases that inform molecular simulations and the engineering of novel receptors.
The study provides mechanistic insight into signal trajectories of LOV photoreceptors and histidine kinases that can inform molecular simulations and engineering of novel receptors.
Taken together, we provide mechanistic insight into the signal trajectories of LOV photoreceptors and histidine kinases that inform molecular simulations and the engineering of novel receptors.
The study provides mechanistic insight into signal trajectories of LOV photoreceptors and histidine kinases that can inform molecular simulations and engineering of novel receptors.
Taken together, we provide mechanistic insight into the signal trajectories of LOV photoreceptors and histidine kinases that inform molecular simulations and the engineering of novel receptors.
The study provides mechanistic insight into signal trajectories of LOV photoreceptors and histidine kinases that can inform molecular simulations and engineering of novel receptors.
Taken together, we provide mechanistic insight into the signal trajectories of LOV photoreceptors and histidine kinases that inform molecular simulations and the engineering of novel receptors.
The study provides mechanistic insight into signal trajectories of LOV photoreceptors and histidine kinases that can inform molecular simulations and engineering of novel receptors.
Taken together, we provide mechanistic insight into the signal trajectories of LOV photoreceptors and histidine kinases that inform molecular simulations and the engineering of novel receptors.
The study provides mechanistic insight into signal trajectories of LOV photoreceptors and histidine kinases that can inform molecular simulations and engineering of novel receptors.
Taken together, we provide mechanistic insight into the signal trajectories of LOV photoreceptors and histidine kinases that inform molecular simulations and the engineering of novel receptors.
The study provides mechanistic insight into signal trajectories of LOV photoreceptors and histidine kinases that can inform molecular simulations and engineering of novel receptors.
Taken together, we provide mechanistic insight into the signal trajectories of LOV photoreceptors and histidine kinases that inform molecular simulations and the engineering of novel receptors.
The study provides mechanistic insight into signal trajectories of LOV photoreceptors and histidine kinases that can inform molecular simulations and engineering of novel receptors.
Taken together, we provide mechanistic insight into the signal trajectories of LOV photoreceptors and histidine kinases that inform molecular simulations and the engineering of novel receptors.
The study provides mechanistic insight into signal trajectories of LOV photoreceptors and histidine kinases that can inform molecular simulations and engineering of novel receptors.
Taken together, we provide mechanistic insight into the signal trajectories of LOV photoreceptors and histidine kinases that inform molecular simulations and the engineering of novel receptors.
In the engineered LOV histidine kinase YF1, blue-light reception involves structural transitions that can be charted by ELDOR spectroscopy and site-directed spin labelling.
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1
In the engineered LOV histidine kinase YF1, blue-light reception involves structural transitions that can be charted by ELDOR spectroscopy and site-directed spin labelling.
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1
In the engineered LOV histidine kinase YF1, blue-light reception involves structural transitions that can be charted by ELDOR spectroscopy and site-directed spin labelling.
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1
In the engineered LOV histidine kinase YF1, blue-light reception involves structural transitions that can be charted by ELDOR spectroscopy and site-directed spin labelling.
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1
In the engineered LOV histidine kinase YF1, blue-light reception involves structural transitions that can be charted by ELDOR spectroscopy and site-directed spin labelling.
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1
In the engineered LOV histidine kinase YF1, blue-light reception involves structural transitions that can be charted by ELDOR spectroscopy and site-directed spin labelling.
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1
In the engineered LOV histidine kinase YF1, blue-light reception involves structural transitions that can be charted by ELDOR spectroscopy and site-directed spin labelling.
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1
In the engineered LOV histidine kinase YF1, blue-light reception involves structural transitions that can be charted by ELDOR spectroscopy and site-directed spin labelling.
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1
In the engineered LOV histidine kinase YF1, blue-light reception involves structural transitions that can be charted by ELDOR spectroscopy and site-directed spin labelling.
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1
In the engineered LOV histidine kinase YF1, blue-light reception involves structural transitions that can be charted by ELDOR spectroscopy and site-directed spin labelling.
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1
In the engineered LOV histidine kinase YF1, blue-light reception involves structural transitions that can be charted by ELDOR spectroscopy and site-directed spin labelling.
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1
In the engineered LOV histidine kinase YF1, blue-light reception involves structural transitions that can be charted by ELDOR spectroscopy and site-directed spin labelling.
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1
In the engineered LOV histidine kinase YF1, blue-light reception involves structural transitions that can be charted by ELDOR spectroscopy and site-directed spin labelling.
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1
In the engineered LOV histidine kinase YF1, blue-light reception involves structural transitions that can be charted by ELDOR spectroscopy and site-directed spin labelling.
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1
In the engineered LOV histidine kinase YF1, blue-light reception involves structural transitions that can be charted by ELDOR spectroscopy and site-directed spin labelling.
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1
In the engineered LOV histidine kinase YF1, blue-light reception involves structural transitions that can be charted by ELDOR spectroscopy and site-directed spin labelling.
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1
In the engineered LOV histidine kinase YF1, blue-light reception involves structural transitions that can be charted by ELDOR spectroscopy and site-directed spin labelling.
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1
Structural modelling based on ELDOR-derived pair-wise distance constraints indicates that light induces rotation and splaying apart of the two LOV photosensors in dimeric YF1.
Structural modelling based on pair-wise distance constraints derived from ELDOR pinpoint light-induced rotation and splaying apart of the two LOV photosensors in the dimeric photoreceptor.
Structural modelling based on ELDOR-derived pair-wise distance constraints indicates that light induces rotation and splaying apart of the two LOV photosensors in dimeric YF1.
Structural modelling based on pair-wise distance constraints derived from ELDOR pinpoint light-induced rotation and splaying apart of the two LOV photosensors in the dimeric photoreceptor.
Structural modelling based on ELDOR-derived pair-wise distance constraints indicates that light induces rotation and splaying apart of the two LOV photosensors in dimeric YF1.
Structural modelling based on pair-wise distance constraints derived from ELDOR pinpoint light-induced rotation and splaying apart of the two LOV photosensors in the dimeric photoreceptor.
Structural modelling based on ELDOR-derived pair-wise distance constraints indicates that light induces rotation and splaying apart of the two LOV photosensors in dimeric YF1.
Structural modelling based on pair-wise distance constraints derived from ELDOR pinpoint light-induced rotation and splaying apart of the two LOV photosensors in the dimeric photoreceptor.
Structural modelling based on ELDOR-derived pair-wise distance constraints indicates that light induces rotation and splaying apart of the two LOV photosensors in dimeric YF1.
Structural modelling based on pair-wise distance constraints derived from ELDOR pinpoint light-induced rotation and splaying apart of the two LOV photosensors in the dimeric photoreceptor.
Structural modelling based on ELDOR-derived pair-wise distance constraints indicates that light induces rotation and splaying apart of the two LOV photosensors in dimeric YF1.
Structural modelling based on pair-wise distance constraints derived from ELDOR pinpoint light-induced rotation and splaying apart of the two LOV photosensors in the dimeric photoreceptor.
Structural modelling based on ELDOR-derived pair-wise distance constraints indicates that light induces rotation and splaying apart of the two LOV photosensors in dimeric YF1.
Structural modelling based on pair-wise distance constraints derived from ELDOR pinpoint light-induced rotation and splaying apart of the two LOV photosensors in the dimeric photoreceptor.
Structural modelling based on ELDOR-derived pair-wise distance constraints indicates that light induces rotation and splaying apart of the two LOV photosensors in dimeric YF1.
Structural modelling based on pair-wise distance constraints derived from ELDOR pinpoint light-induced rotation and splaying apart of the two LOV photosensors in the dimeric photoreceptor.
Structural modelling based on ELDOR-derived pair-wise distance constraints indicates that light induces rotation and splaying apart of the two LOV photosensors in dimeric YF1.
Structural modelling based on pair-wise distance constraints derived from ELDOR pinpoint light-induced rotation and splaying apart of the two LOV photosensors in the dimeric photoreceptor.
Structural modelling based on ELDOR-derived pair-wise distance constraints indicates that light induces rotation and splaying apart of the two LOV photosensors in dimeric YF1.
Structural modelling based on pair-wise distance constraints derived from ELDOR pinpoint light-induced rotation and splaying apart of the two LOV photosensors in the dimeric photoreceptor.
Structural modelling based on ELDOR-derived pair-wise distance constraints indicates that light induces rotation and splaying apart of the two LOV photosensors in dimeric YF1.
Structural modelling based on pair-wise distance constraints derived from ELDOR pinpoint light-induced rotation and splaying apart of the two LOV photosensors in the dimeric photoreceptor.
Structural modelling based on ELDOR-derived pair-wise distance constraints indicates that light induces rotation and splaying apart of the two LOV photosensors in dimeric YF1.
Structural modelling based on pair-wise distance constraints derived from ELDOR pinpoint light-induced rotation and splaying apart of the two LOV photosensors in the dimeric photoreceptor.
Structural modelling based on ELDOR-derived pair-wise distance constraints indicates that light induces rotation and splaying apart of the two LOV photosensors in dimeric YF1.
Structural modelling based on pair-wise distance constraints derived from ELDOR pinpoint light-induced rotation and splaying apart of the two LOV photosensors in the dimeric photoreceptor.
Structural modelling based on ELDOR-derived pair-wise distance constraints indicates that light induces rotation and splaying apart of the two LOV photosensors in dimeric YF1.
Structural modelling based on pair-wise distance constraints derived from ELDOR pinpoint light-induced rotation and splaying apart of the two LOV photosensors in the dimeric photoreceptor.
Structural modelling based on ELDOR-derived pair-wise distance constraints indicates that light induces rotation and splaying apart of the two LOV photosensors in dimeric YF1.
Structural modelling based on pair-wise distance constraints derived from ELDOR pinpoint light-induced rotation and splaying apart of the two LOV photosensors in the dimeric photoreceptor.
Structural modelling based on ELDOR-derived pair-wise distance constraints indicates that light induces rotation and splaying apart of the two LOV photosensors in dimeric YF1.
Structural modelling based on pair-wise distance constraints derived from ELDOR pinpoint light-induced rotation and splaying apart of the two LOV photosensors in the dimeric photoreceptor.
Structural modelling based on ELDOR-derived pair-wise distance constraints indicates that light induces rotation and splaying apart of the two LOV photosensors in dimeric YF1.
Structural modelling based on pair-wise distance constraints derived from ELDOR pinpoint light-induced rotation and splaying apart of the two LOV photosensors in the dimeric photoreceptor.
The molecular strain generated by light-induced photosensor rearrangement likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
Resultant molecular strain likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
The molecular strain generated by light-induced photosensor rearrangement likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
Resultant molecular strain likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
The molecular strain generated by light-induced photosensor rearrangement likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
Resultant molecular strain likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
The molecular strain generated by light-induced photosensor rearrangement likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
Resultant molecular strain likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
The molecular strain generated by light-induced photosensor rearrangement likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
Resultant molecular strain likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
The molecular strain generated by light-induced photosensor rearrangement likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
Resultant molecular strain likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
The molecular strain generated by light-induced photosensor rearrangement likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
Resultant molecular strain likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
The molecular strain generated by light-induced photosensor rearrangement likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
Resultant molecular strain likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
The molecular strain generated by light-induced photosensor rearrangement likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
Resultant molecular strain likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
The molecular strain generated by light-induced photosensor rearrangement likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
Resultant molecular strain likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
Approval Evidence
1 source3 linked approval claimsfirst-pass slug electron-electron-double-resonance-spectroscopy
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling
Source:
comparative mechanismsupports
A photoreceptor variant with an inverted signal response has a drastically altered dimer interface but shows linker structural transitions similar to those in YF1 under light stimulation.
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
Source:
mechanistic insightsupports
In the engineered LOV histidine kinase YF1, blue-light reception involves structural transitions that can be charted by ELDOR spectroscopy and site-directed spin labelling.
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1
Source:
structural mechanismsupports
Structural modelling based on ELDOR-derived pair-wise distance constraints indicates that light induces rotation and splaying apart of the two LOV photosensors in dimeric YF1.
Structural modelling based on pair-wise distance constraints derived from ELDOR pinpoint light-induced rotation and splaying apart of the two LOV photosensors in the dimeric photoreceptor.
Source:
Comparisons
Source-backed strengths
In the cited application, ELDOR spectroscopy with site-directed spin labelling yielded mechanistic insight into blue-light reception through quaternary transitions in YF1. The study also reports that a photoreceptor variant with inverted signal response had a drastically altered dimer interface while retaining linker structural transitions similar to YF1, supporting the method's ability to distinguish interface-level rearrangements from shared linker motions.
Source:
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
Compared with light-oxygen-voltage sensing (LOV) domain
electron-electron double resonance spectroscopy and light-oxygen-voltage sensing (LOV) domain address a similar problem space because they share signaling.
Shared frame: shared target processes: signaling; shared mechanisms: heterodimerization; same primary input modality: light
Compared with site-directed spin labelling
electron-electron double resonance spectroscopy and site-directed spin labelling address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; shared mechanisms: light-induced conformational switching, quaternary structural rearrangement; same primary input modality: light
Compared with tandem-dimer nano (tdnano)
electron-electron double resonance spectroscopy and tandem-dimer nano (tdnano) address a similar problem space because they share signaling.
Shared frame: shared target processes: signaling; shared mechanisms: heterodimerization; same primary input modality: light
Strengths here: looks easier to implement in practice.
Ranked Citations
- 1.