Source 1review2010Protein Science
Toolkit/joining proteins in creative ways
joining proteins in creative ways
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
"Joining proteins in creative ways" is a protein engineering construct pattern in which protein domains are fused or otherwise combined to create stimulus-coupled conformational switching in proteins that previously lacked such behavior. The cited literature presents this strategy as a route to generate switchable proteins for biosensing and regulated biological function.
Usefulness & Problems
Why this is useful
This design pattern is useful because it enables the conversion of non-switching proteins into conformational switches that respond to signaling events. The cited application space includes reagent-free biosensors and proteins with regulated biological functions.
Source:
Proteins that switch conformations in response to a signaling event (e.g., ligand binding or chemical modification) present a unique solution to the design of reagent-free biosensors as well as molecules whose biological functions are regulated in useful ways.
Problem solved
It addresses the engineering problem of introducing switching behavior into proteins, particularly binding proteins that do not naturally undergo the desired conformational transitions. The literature specifically frames this as creating proteins whose activity or state can be coupled to signaling inputs.
Source:
Proteins that switch conformations in response to a signaling event (e.g., ligand binding or chemical modification) present a unique solution to the design of reagent-free biosensors as well as molecules whose biological functions are regulated in useful ways.
Problem links
Need conditional recombination or state switching
Derived“Joining proteins in creative ways” describes a construct design pattern in which protein domains are fused or combined to introduce stimulus-coupled conformational switching into proteins that previously lacked such behavior. The cited literature frames this strategy as a route to create switchable proteins for biosensing and regulated biological function.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A reusable architecture pattern for arranging parts into an engineered system.
Mechanisms
allosteric couplingallosteric couplingconformational uncagingconformational uncagingConformational UncagingTechniques
No technique tags yet.
Target processes
recombinationImplementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationoperating role: actuatoroperating role: sensorswitch architecture: uncaging
Implementation is described only at the level of combining or joining proteins to leverage or create switching behavior. The supplied evidence does not specify cofactors, host systems, linker design, delivery methods, or construct optimization details.
The supplied evidence is high-level and does not identify specific fusion architectures, target proteins, signaling inputs, or measured performance. No direct validation for recombination-related applications is provided in the evidence set.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Proteins engineered to switch conformation in response to signaling events can serve as reagent-free biosensors and as molecules with regulated biological functions.
Proteins that switch conformations in response to a signaling event (e.g., ligand binding or chemical modification) present a unique solution to the design of reagent-free biosensors as well as molecules whose biological functions are regulated in useful ways.
Proteins engineered to switch conformation in response to signaling events can serve as reagent-free biosensors and as molecules with regulated biological functions.
Proteins that switch conformations in response to a signaling event (e.g., ligand binding or chemical modification) present a unique solution to the design of reagent-free biosensors as well as molecules whose biological functions are regulated in useful ways.
Proteins engineered to switch conformation in response to signaling events can serve as reagent-free biosensors and as molecules with regulated biological functions.
Proteins that switch conformations in response to a signaling event (e.g., ligand binding or chemical modification) present a unique solution to the design of reagent-free biosensors as well as molecules whose biological functions are regulated in useful ways.
Proteins engineered to switch conformation in response to signaling events can serve as reagent-free biosensors and as molecules with regulated biological functions.
Proteins that switch conformations in response to a signaling event (e.g., ligand binding or chemical modification) present a unique solution to the design of reagent-free biosensors as well as molecules whose biological functions are regulated in useful ways.
Proteins engineered to switch conformation in response to signaling events can serve as reagent-free biosensors and as molecules with regulated biological functions.
Proteins that switch conformations in response to a signaling event (e.g., ligand binding or chemical modification) present a unique solution to the design of reagent-free biosensors as well as molecules whose biological functions are regulated in useful ways.
Proteins engineered to switch conformation in response to signaling events can serve as reagent-free biosensors and as molecules with regulated biological functions.
Proteins that switch conformations in response to a signaling event (e.g., ligand binding or chemical modification) present a unique solution to the design of reagent-free biosensors as well as molecules whose biological functions are regulated in useful ways.
Proteins engineered to switch conformation in response to signaling events can serve as reagent-free biosensors and as molecules with regulated biological functions.
Proteins that switch conformations in response to a signaling event (e.g., ligand binding or chemical modification) present a unique solution to the design of reagent-free biosensors as well as molecules whose biological functions are regulated in useful ways.
Proteins engineered to switch conformation in response to signaling events can serve as reagent-free biosensors and as molecules with regulated biological functions.
Proteins that switch conformations in response to a signaling event (e.g., ligand binding or chemical modification) present a unique solution to the design of reagent-free biosensors as well as molecules whose biological functions are regulated in useful ways.
Proteins engineered to switch conformation in response to signaling events can serve as reagent-free biosensors and as molecules with regulated biological functions.
Proteins that switch conformations in response to a signaling event (e.g., ligand binding or chemical modification) present a unique solution to the design of reagent-free biosensors as well as molecules whose biological functions are regulated in useful ways.
Proteins engineered to switch conformation in response to signaling events can serve as reagent-free biosensors and as molecules with regulated biological functions.
Proteins that switch conformations in response to a signaling event (e.g., ligand binding or chemical modification) present a unique solution to the design of reagent-free biosensors as well as molecules whose biological functions are regulated in useful ways.
Proteins engineered to switch conformation in response to signaling events can serve as reagent-free biosensors and as molecules with regulated biological functions.
Proteins that switch conformations in response to a signaling event (e.g., ligand binding or chemical modification) present a unique solution to the design of reagent-free biosensors as well as molecules whose biological functions are regulated in useful ways.
Proteins engineered to switch conformation in response to signaling events can serve as reagent-free biosensors and as molecules with regulated biological functions.
Proteins that switch conformations in response to a signaling event (e.g., ligand binding or chemical modification) present a unique solution to the design of reagent-free biosensors as well as molecules whose biological functions are regulated in useful ways.
Proteins engineered to switch conformation in response to signaling events can serve as reagent-free biosensors and as molecules with regulated biological functions.
Proteins that switch conformations in response to a signaling event (e.g., ligand binding or chemical modification) present a unique solution to the design of reagent-free biosensors as well as molecules whose biological functions are regulated in useful ways.
Proteins engineered to switch conformation in response to signaling events can serve as reagent-free biosensors and as molecules with regulated biological functions.
Proteins that switch conformations in response to a signaling event (e.g., ligand binding or chemical modification) present a unique solution to the design of reagent-free biosensors as well as molecules whose biological functions are regulated in useful ways.
Proteins engineered to switch conformation in response to signaling events can serve as reagent-free biosensors and as molecules with regulated biological functions.
Proteins that switch conformations in response to a signaling event (e.g., ligand binding or chemical modification) present a unique solution to the design of reagent-free biosensors as well as molecules whose biological functions are regulated in useful ways.
Proteins engineered to switch conformation in response to signaling events can serve as reagent-free biosensors and as molecules with regulated biological functions.
Proteins that switch conformations in response to a signaling event (e.g., ligand binding or chemical modification) present a unique solution to the design of reagent-free biosensors as well as molecules whose biological functions are regulated in useful ways.
Proteins engineered to switch conformation in response to signaling events can serve as reagent-free biosensors and as molecules with regulated biological functions.
Proteins that switch conformations in response to a signaling event (e.g., ligand binding or chemical modification) present a unique solution to the design of reagent-free biosensors as well as molecules whose biological functions are regulated in useful ways.
Proteins engineered to switch conformation in response to signaling events can serve as reagent-free biosensors and as molecules with regulated biological functions.
Proteins that switch conformations in response to a signaling event (e.g., ligand binding or chemical modification) present a unique solution to the design of reagent-free biosensors as well as molecules whose biological functions are regulated in useful ways.
Proteins engineered to switch conformation in response to signaling events can serve as reagent-free biosensors and as molecules with regulated biological functions.
Proteins that switch conformations in response to a signaling event (e.g., ligand binding or chemical modification) present a unique solution to the design of reagent-free biosensors as well as molecules whose biological functions are regulated in useful ways.
Proteins engineered to switch conformation in response to signaling events can serve as reagent-free biosensors and as molecules with regulated biological functions.
Proteins that switch conformations in response to a signaling event (e.g., ligand binding or chemical modification) present a unique solution to the design of reagent-free biosensors as well as molecules whose biological functions are regulated in useful ways.
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
A major obstacle to developing such switching proteins is that most natural proteins do not undergo conformational change upon ligand binding or chemical modification.
The principal roadblock in the path to develop such molecules is that the majority of natural proteins do not change conformation upon binding their cognate ligands or becoming chemically modified.
A major obstacle to developing such switching proteins is that most natural proteins do not undergo conformational change upon ligand binding or chemical modification.
The principal roadblock in the path to develop such molecules is that the majority of natural proteins do not change conformation upon binding their cognate ligands or becoming chemically modified.
A major obstacle to developing such switching proteins is that most natural proteins do not undergo conformational change upon ligand binding or chemical modification.
The principal roadblock in the path to develop such molecules is that the majority of natural proteins do not change conformation upon binding their cognate ligands or becoming chemically modified.
A major obstacle to developing such switching proteins is that most natural proteins do not undergo conformational change upon ligand binding or chemical modification.
The principal roadblock in the path to develop such molecules is that the majority of natural proteins do not change conformation upon binding their cognate ligands or becoming chemically modified.
A major obstacle to developing such switching proteins is that most natural proteins do not undergo conformational change upon ligand binding or chemical modification.
The principal roadblock in the path to develop such molecules is that the majority of natural proteins do not change conformation upon binding their cognate ligands or becoming chemically modified.
A major obstacle to developing such switching proteins is that most natural proteins do not undergo conformational change upon ligand binding or chemical modification.
The principal roadblock in the path to develop such molecules is that the majority of natural proteins do not change conformation upon binding their cognate ligands or becoming chemically modified.
A major obstacle to developing such switching proteins is that most natural proteins do not undergo conformational change upon ligand binding or chemical modification.
The principal roadblock in the path to develop such molecules is that the majority of natural proteins do not change conformation upon binding their cognate ligands or becoming chemically modified.
A major obstacle to developing such switching proteins is that most natural proteins do not undergo conformational change upon ligand binding or chemical modification.
The principal roadblock in the path to develop such molecules is that the majority of natural proteins do not change conformation upon binding their cognate ligands or becoming chemically modified.
A major obstacle to developing such switching proteins is that most natural proteins do not undergo conformational change upon ligand binding or chemical modification.
The principal roadblock in the path to develop such molecules is that the majority of natural proteins do not change conformation upon binding their cognate ligands or becoming chemically modified.
A major obstacle to developing such switching proteins is that most natural proteins do not undergo conformational change upon ligand binding or chemical modification.
The principal roadblock in the path to develop such molecules is that the majority of natural proteins do not change conformation upon binding their cognate ligands or becoming chemically modified.
A major obstacle to developing such switching proteins is that most natural proteins do not undergo conformational change upon ligand binding or chemical modification.
The principal roadblock in the path to develop such molecules is that the majority of natural proteins do not change conformation upon binding their cognate ligands or becoming chemically modified.
A major obstacle to developing such switching proteins is that most natural proteins do not undergo conformational change upon ligand binding or chemical modification.
The principal roadblock in the path to develop such molecules is that the majority of natural proteins do not change conformation upon binding their cognate ligands or becoming chemically modified.
A major obstacle to developing such switching proteins is that most natural proteins do not undergo conformational change upon ligand binding or chemical modification.
The principal roadblock in the path to develop such molecules is that the majority of natural proteins do not change conformation upon binding their cognate ligands or becoming chemically modified.
A major obstacle to developing such switching proteins is that most natural proteins do not undergo conformational change upon ligand binding or chemical modification.
The principal roadblock in the path to develop such molecules is that the majority of natural proteins do not change conformation upon binding their cognate ligands or becoming chemically modified.
A major obstacle to developing such switching proteins is that most natural proteins do not undergo conformational change upon ligand binding or chemical modification.
The principal roadblock in the path to develop such molecules is that the majority of natural proteins do not change conformation upon binding their cognate ligands or becoming chemically modified.
A major obstacle to developing such switching proteins is that most natural proteins do not undergo conformational change upon ligand binding or chemical modification.
The principal roadblock in the path to develop such molecules is that the majority of natural proteins do not change conformation upon binding their cognate ligands or becoming chemically modified.
A major obstacle to developing such switching proteins is that most natural proteins do not undergo conformational change upon ligand binding or chemical modification.
The principal roadblock in the path to develop such molecules is that the majority of natural proteins do not change conformation upon binding their cognate ligands or becoming chemically modified.
A major obstacle to developing such switching proteins is that most natural proteins do not undergo conformational change upon ligand binding or chemical modification.
The principal roadblock in the path to develop such molecules is that the majority of natural proteins do not change conformation upon binding their cognate ligands or becoming chemically modified.
A major obstacle to developing such switching proteins is that most natural proteins do not undergo conformational change upon ligand binding or chemical modification.
The principal roadblock in the path to develop such molecules is that the majority of natural proteins do not change conformation upon binding their cognate ligands or becoming chemically modified.
A major obstacle to developing such switching proteins is that most natural proteins do not undergo conformational change upon ligand binding or chemical modification.
The principal roadblock in the path to develop such molecules is that the majority of natural proteins do not change conformation upon binding their cognate ligands or becoming chemically modified.
Approval Evidence
1 source1 linked approval claimfirst-pass slug joining-proteins-in-creative-ways
By ... joining proteins in creative ways ... researchers are learning how to coax conformational changes from proteins that previously had none.
Source:
engineering strategy overviewsupports
Recent protein engineering efforts introduce switching properties into binding proteins by leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Source:
Comparisons
Source-backed strengths
A key strength is conceptual generality: the cited review describes joining proteins as one of the strategies used to induce conformational changes in otherwise non-switching proteins. It is also positioned as enabling both sensing and functional regulation, but no quantitative performance metrics are provided in the supplied evidence.
Source:
Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none.
Compared with antisense oligodeoxynucleotide against Per1
joining proteins in creative ways and antisense oligodeoxynucleotide against Per1 address a similar problem space because they share recombination.
Shared frame: same top-level item type; shared target processes: recombination
Strengths here: looks easier to implement in practice.
Compared with Opto-Casp8-V2
joining proteins in creative ways and Opto-Casp8-V2 address a similar problem space because they share recombination.
Shared frame: same top-level item type; shared target processes: recombination
Strengths here: looks easier to implement in practice.
Compared with red light-inducible recombinase library
joining proteins in creative ways and red light-inducible recombinase library address a similar problem space because they share recombination.
Shared frame: same top-level item type; shared target processes: recombination
Strengths here: looks easier to implement in practice.
Ranked Citations
- 1.