Source 1primary paper2017Scientific Reports
Toolkit/site-directed spin labelling
site-directed spin labelling
Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Site-directed spin labelling, used with electron-electron double resonance (ELDOR) spectroscopy, is a structural assay method for charting blue-light-induced conformational changes in proteins. In the cited study, it was applied to the engineered LOV histidine kinase YF1 to obtain distance information on light-dependent structural transitions and quaternary rearrangements.
Usefulness & Problems
Why this is useful
This method is useful for mapping light-dependent structural trajectories in signaling proteins when conformational changes must be inferred from pairwise distance constraints. The cited work indicates that the resulting mechanistic insight can inform structural modelling, molecular simulations, and engineering of LOV photoreceptors and histidine kinases.
Problem solved
It addresses the problem of experimentally resolving how blue-light reception is coupled to structural transitions in an engineered LOV histidine kinase. Specifically, it enables charting conformational and quaternary changes in YF1 under light stimulation using distance-sensitive spectroscopy.
Problem links
Need conditional control of signaling activity
DerivedSite-directed spin labelling, used together with electron-electron double resonance (ELDOR) spectroscopy, is an assay method for mapping light-dependent structural changes in proteins. In the cited work, it was applied to the engineered LOV histidine kinase YF1 to chart blue-light-induced conformational transitions and derive pairwise distance constraints for structural modelling.
Need precise spatiotemporal control with light input
DerivedSite-directed spin labelling, used together with electron-electron double resonance (ELDOR) spectroscopy, is an assay method for mapping light-dependent structural changes in proteins. In the cited work, it was applied to the engineered LOV histidine kinase YF1 to chart blue-light-induced conformational transitions and derive pairwise distance constraints for structural modelling.
Taxonomy & Function
Primary hierarchy
Technique Branch
Method: A concrete measurement method used to characterize an engineered system.
Mechanisms
electron-electron double resonance distance measurementelectron-electron double resonance distance measurementlight-induced conformational switchinglight-induced conformational switchingquaternary structural rearrangementquaternary structural rearrangementsite-directed spin labellingsite-directed spin labellingTarget processes
signalingInput: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: spectral hardware requirementoperating role: sensor
The available evidence specifies use of site-directed spin labelling together with electron-electron double resonance (ELDOR) spectroscopy under blue-light stimulation. Beyond this pairing and its application to YF1, the supplied material does not provide practical details on construct design, spin-label identity, expression system, or sample preparation.
The supplied evidence is limited to a single cited study and primarily supports use in the engineered LOV histidine kinase YF1 and a related photoreceptor variant. The evidence provided does not specify labeling chemistry, distance range, temporal resolution, or performance across diverse protein classes.
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.
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.
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 source1 linked approval claimfirst-pass slug site-directed-spin-labelling
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling
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:
Comparisons
Source-backed strengths
The cited study supports that site-directed spin labelling combined with ELDOR can detect light-dependent structural transitions in YF1 and relate them to quaternary rearrangements. It also supported comparative mechanistic analysis, because a photoreceptor variant with inverted signal response showed a drastically altered dimer interface while retaining linker transitions similar to YF1.
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 cDNA microarray
site-directed spin labelling and cDNA microarray address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; same primary input modality: light
Compared with electron-electron double resonance spectroscopy
site-directed spin labelling and electron-electron double resonance spectroscopy 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 IRAP-pHluorin translocation assay
site-directed spin labelling and IRAP-pHluorin translocation assay address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; same primary input modality: light
Ranked Citations
- 1.