Source 1primary paper2020Scientific Reports
Toolkit/Aureochrome1a LOV domain
Aureochrome1a LOV domain
Also known as: a LOV domain of aureochrome1a from Phaeodactylum tricornutum
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The Aureochrome1a LOV domain from Phaeodactylum tricornutum is a flavin-binding blue-light sensory protein domain used as the basis for designed LOV-domain flavoproteins. In the cited 2020 Scientific Reports study, tailored LOV-domain flavoproteins produced nuclear hyperpolarization upon illumination, functioning as light-driven spin machines.
Usefulness & Problems
Why this is useful
This domain is useful as a flavoprotein photosensory scaffold for engineering light-driven nuclear hyperpolarization. The supplied evidence supports its use in designed spin-active protein systems, but does not provide broader application benchmarks.
Problem solved
It helps address the problem of generating nuclear hyperpolarization using an illuminated protein-based molecular system. The evidence specifically supports light-driven production of nuclear hyperpolarization by designed LOV-domain flavoproteins.
Published Workflows
Objective: Design LOV-domain flavoproteins that act as light-driven spin machines producing nuclear hyperpolarization upon illumination.
Why it works: The abstract states that illumination drives FMN to abstract an electron from tryptophan, forming a transient spin-correlated radical pair that generates the photo-CIDNP effect.
FMN-mediated electron abstraction from tryptophantransient spin-correlated radical pair formationheuristic biomimetic designliquid-state high-resolution NMR readout
Stages
- 1.Biomimetic LOV-domain design(library_design)
The abstract describes a heuristic biomimetic design strategy using LOV domains and tryptophan engineering to create molecular spin machines.
Selection: Choose LOV-domain flavoprotein scaffolds and engineer tryptophan placement to enable photo-CIDNP-generating radical-pair chemistry.
- 2.NMR-based observation of photo-CIDNP(confirmatory_validation)
The abstract uses NMR observation as the evidence that the engineered designs produce photo-CIDNP and to infer magnetic interaction features.
Selection: Observe photo-CIDNP effects by 15N and 1H liquid-state high-resolution NMR.
Steps
- 1.Select LOV-domain scaffolds for spin-machine designengineered protein scaffolds
Use LOV-domain flavoproteins as the basis for designed molecular spin machines.
Scaffold choice precedes residue-level engineering because the design is framed around specific LOV-domain proteins.
- 2.Insert tryptophan at canonical and novel positions in Mr4511engineered protein scaffold
Create the tryptophan-containing design needed for the reported photo-CIDNP effect in Mr4511.
The abstract identifies tryptophan insertion as the engineering change that enables the observed effect in a scaffold whose wild-type form lacks the otherwise conserved tryptophan.
- 3.Measure engineered variants by 15N and 1H liquid-state high-resolution NMRengineered construct and assay readout
Observe whether the engineered variants yield photo-CIDNP effects and assess magnetic-field dependence.
NMR is used after design to confirm that the engineered proteins produce the intended hyperpolarization behavior.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
anisotropic magnetic interactions in a transient paramagnetic statelight-driven nuclear hyperpolarizationphoto-cidnpTechniques
Computational DesignTarget processes
No target processes tagged yet.
Implementation Constraints
This tool is a LOV flavoprotein domain derived from Aureochrome1a of Phaeodactylum tricornutum and therefore relies on a flavin-binding photosensory module. Beyond its use in designed LOV-domain flavoproteins in the cited study, the provided evidence does not describe construct design, expression conditions, or delivery requirements.
The supplied evidence is limited to a single cited study and a single functional claim. It does not specify illumination wavelength, magnitude of hyperpolarization, construct architecture, host system, or independent replication.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Insertion of tryptophan at canonical and novel positions in Mr4511 yields photo-CIDNP effects detectable by 15N and 1H liquid-state high-resolution NMR.
Insertion of the tryptophan at canonical and novel positions in Mr4511 yields photo-CIDNP effects observed by 15N and 1H liquid-state high-resolution NMR
Insertion of tryptophan at canonical and novel positions in Mr4511 yields photo-CIDNP effects detectable by 15N and 1H liquid-state high-resolution NMR.
Insertion of the tryptophan at canonical and novel positions in Mr4511 yields photo-CIDNP effects observed by 15N and 1H liquid-state high-resolution NMR
Insertion of tryptophan at canonical and novel positions in Mr4511 yields photo-CIDNP effects detectable by 15N and 1H liquid-state high-resolution NMR.
Insertion of the tryptophan at canonical and novel positions in Mr4511 yields photo-CIDNP effects observed by 15N and 1H liquid-state high-resolution NMR
Insertion of tryptophan at canonical and novel positions in Mr4511 yields photo-CIDNP effects detectable by 15N and 1H liquid-state high-resolution NMR.
Insertion of the tryptophan at canonical and novel positions in Mr4511 yields photo-CIDNP effects observed by 15N and 1H liquid-state high-resolution NMR
Insertion of tryptophan at canonical and novel positions in Mr4511 yields photo-CIDNP effects detectable by 15N and 1H liquid-state high-resolution NMR.
Insertion of the tryptophan at canonical and novel positions in Mr4511 yields photo-CIDNP effects observed by 15N and 1H liquid-state high-resolution NMR
Designed LOV-domain flavoproteins can produce nuclear hyperpolarization upon illumination.
Here, we report on designed molecular spin-machines producing nuclear hyperpolarization upon illumination
Designed LOV-domain flavoproteins can produce nuclear hyperpolarization upon illumination.
Here, we report on designed molecular spin-machines producing nuclear hyperpolarization upon illumination
Designed LOV-domain flavoproteins can produce nuclear hyperpolarization upon illumination.
Here, we report on designed molecular spin-machines producing nuclear hyperpolarization upon illumination
Designed LOV-domain flavoproteins can produce nuclear hyperpolarization upon illumination.
Here, we report on designed molecular spin-machines producing nuclear hyperpolarization upon illumination
Designed LOV-domain flavoproteins can produce nuclear hyperpolarization upon illumination.
Here, we report on designed molecular spin-machines producing nuclear hyperpolarization upon illumination
The magnetic-field dependence of the observed photo-CIDNP effects indicates involvement of anisotropic magnetic interactions and a slow-motion regime in the transient paramagnetic state.
with a characteristic magnetic-field dependence indicating an involvement of anisotropic magnetic interactions and a slow-motion regime in the transient paramagnetic state
The magnetic-field dependence of the observed photo-CIDNP effects indicates involvement of anisotropic magnetic interactions and a slow-motion regime in the transient paramagnetic state.
with a characteristic magnetic-field dependence indicating an involvement of anisotropic magnetic interactions and a slow-motion regime in the transient paramagnetic state
The magnetic-field dependence of the observed photo-CIDNP effects indicates involvement of anisotropic magnetic interactions and a slow-motion regime in the transient paramagnetic state.
with a characteristic magnetic-field dependence indicating an involvement of anisotropic magnetic interactions and a slow-motion regime in the transient paramagnetic state
The magnetic-field dependence of the observed photo-CIDNP effects indicates involvement of anisotropic magnetic interactions and a slow-motion regime in the transient paramagnetic state.
with a characteristic magnetic-field dependence indicating an involvement of anisotropic magnetic interactions and a slow-motion regime in the transient paramagnetic state
The magnetic-field dependence of the observed photo-CIDNP effects indicates involvement of anisotropic magnetic interactions and a slow-motion regime in the transient paramagnetic state.
with a characteristic magnetic-field dependence indicating an involvement of anisotropic magnetic interactions and a slow-motion regime in the transient paramagnetic state
Approval Evidence
1 source1 linked approval claimfirst-pass slug aureochrome1a-lov-domain
Here, we report on designed molecular spin-machines producing nuclear hyperpolarization upon illumination: a LOV domain of aureochrome1a from Phaeodactylum tricornutum
Source:
functional capabilitysupports
Designed LOV-domain flavoproteins can produce nuclear hyperpolarization upon illumination.
Here, we report on designed molecular spin-machines producing nuclear hyperpolarization upon illumination
Source:
Comparisons
Source-backed strengths
The key demonstrated strength is that tailored LOV-domain flavoproteins based on this LOV scaffold can produce nuclear hyperpolarization upon illumination. The evidence links this capability to a defined flavin-binding light-sensing domain from Phaeodactylum tricornutum.
Ranked Citations
- 1.