Source 1review2010Protein Science
Toolkit/co-opting natural allosteric coupling
co-opting natural allosteric coupling
Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Co-opting natural allosteric coupling is a protein engineering method that converts proteins into conformational switches by leveraging pre-existing allosteric relationships. The cited literature describes its use to generate proteins that respond to signaling events and thereby enable biosensing or regulated biological function.
Usefulness & Problems
Why this is useful
This method is useful for introducing switch-like behavior into proteins that previously lacked such conformational regulation. The cited review specifically positions these engineered switches as reagent-free biosensors and as molecules 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 challenge of endowing otherwise non-switching proteins, including binding proteins, with signal-responsive conformational changes. This enables control of protein function by signaling events without requiring external reagents in the biosensing context described.
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
DerivedCo-opting natural allosteric coupling is a protein engineering method that introduces switching behavior into proteins by leveraging pre-existing allosteric relationships. The cited literature describes its use to coax conformational changes from proteins that previously lacked such switching and to create proteins whose functions can be regulated by signaling events.
Taxonomy & Function
Primary hierarchy
Technique Branch
Method: A concrete method used to build, optimize, or evolve an engineered system.
Mechanisms
allosteric couplingallosteric couplingconformational switchingconformational switchingconformational uncagingconformational uncagingConformational UncagingTechniques
No technique tags yet.
Target processes
recombinationImplementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationoperating role: builderswitch architecture: uncaging
The evidence indicates that the method is applied through protein engineering and is discussed alongside strategies such as joining proteins and creating new switching mechanisms. However, the provided material does not specify construct architectures, host systems, cofactors, or assay formats for implementation.
The supplied evidence is limited to a general review-level description and does not provide specific proteins, quantitative performance metrics, or direct validation in recombination systems. Practical constraints, generality across protein classes, and comparative performance versus other switching strategies are not described in the provided evidence.
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 co-opting-natural-allosteric-coupling
By co-opting natural allosteric coupling ... 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 that the strategy exploits natural allosteric coupling already present in proteins rather than requiring an entirely de novo switching mechanism. The cited literature states that this approach can coax conformational changes from proteins that previously had none and can support biosensing and functional regulation applications.
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 multiplexed engineering
co-opting natural allosteric coupling and multiplexed engineering address a similar problem space because they share recombination.
Shared frame: same top-level item type; shared target processes: recombination
Compared with new switching mechanisms
co-opting natural allosteric coupling and new switching mechanisms address a similar problem space because they share recombination.
Shared frame: same top-level item type; shared target processes: recombination; shared mechanisms: conformational switching, conformational uncaging, conformational_uncaging
Compared with shRNA-delivered by lentivirus
co-opting natural allosteric coupling and shRNA-delivered by lentivirus address a similar problem space because they share recombination.
Shared frame: same top-level item type; shared target processes: recombination
Ranked Citations
- 1.