Source 1primary paper2020Biophysical Chemistry
Toolkit/LOV2 domain C450A variant
LOV2 domain C450A variant
Also known as: C450A variant
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The LOV2 domain C450A variant is a mutant form of the LOV2 photosensory domain that has been examined for its conformational properties across a broad pH range. The available evidence supports biophysical characterization of this variant rather than a demonstrated engineered application.
Usefulness & Problems
Why this is useful
This variant is useful as a biophysical comparison point for understanding how mutation and pH influence LOV2-domain conformational behavior. The supplied evidence does not document a specific applied use beyond this characterization context.
Problem solved
The reported work addresses the problem of characterizing conformational properties of the LOV2 domain and its C450A variant over a broad pH region. No evidence is provided for solving a downstream cellular, optogenetic, or protein-engineering application problem.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Techniques
No technique tags yet.
Target processes
No target processes tagged yet.
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationoperating role: actuatorswitch architecture: uncaging
The available evidence identifies this tool as a C450A mutant of the LOV2 domain, implying generation by amino-acid substitution. No further practical details are provided on construct design, cofactors, expression system, illumination conditions, or assay implementation.
The evidence is limited to a single study title describing conformational-property analysis, with no detailed results, assay outputs, or application data. There is no supplied evidence for light-controlled performance, cellular validation, or independent replication.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
The paper studies conformational properties of the LOV2 domain and its C450A variant across a broad pH region.
The paper studies conformational properties of the LOV2 domain and its C450A variant across a broad pH region.
The paper studies conformational properties of the LOV2 domain and its C450A variant across a broad pH region.
The paper studies conformational properties of the LOV2 domain and its C450A variant across a broad pH region.
The paper studies conformational properties of the LOV2 domain and its C450A variant across a broad pH region.
The paper studies conformational properties of the LOV2 domain and its C450A variant across a broad pH region.
The paper studies conformational properties of the LOV2 domain and its C450A variant across a broad pH region.
The paper studies conformational properties of the LOV2 domain and its C450A variant across a broad pH region.
The paper studies conformational properties of the LOV2 domain and its C450A variant across a broad pH region.
The paper studies conformational properties of the LOV2 domain and its C450A variant across a broad pH region.
The paper studies conformational properties of the LOV2 domain and its C450A variant across a broad pH region.
The paper studies conformational properties of the LOV2 domain and its C450A variant across a broad pH region.
The paper studies conformational properties of the LOV2 domain and its C450A variant across a broad pH region.
The paper studies conformational properties of the LOV2 domain and its C450A variant across a broad pH region.
The paper studies conformational properties of the LOV2 domain and its C450A variant across a broad pH region.
The paper studies conformational properties of the LOV2 domain and its C450A variant across a broad pH region.
The paper studies conformational properties of the LOV2 domain and its C450A variant across a broad pH region.
Approval Evidence
1 source1 linked approval claimfirst-pass slug lov2-domain-c450a-variant
Conformational properties of LOV2 domain and its C450A variant within broad pH region
Source:
study focussupports
The paper studies conformational properties of the LOV2 domain and its C450A variant across a broad pH region.
Source:
Comparisons
Source-backed strengths
A stated strength is that the variant was studied across a broad pH region, which supports analysis of conformational behavior under multiple chemical conditions. Beyond this scope of characterization, the supplied evidence does not report performance benchmarks or functional validation.
Compared with anion channelrhodopsins
LOV2 domain C450A variant and anion channelrhodopsins address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: conformational_uncaging
Strengths here: looks easier to implement in practice.
Compared with AUREO1 LOV-only construct
LOV2 domain C450A variant and AUREO1 LOV-only construct address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: conformational_uncaging
Strengths here: looks easier to implement in practice.
Compared with CIB1 helix 10 pocket
LOV2 domain C450A variant and CIB1 helix 10 pocket address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: conformational uncaging, conformational_uncaging
Ranked Citations
- 1.