Source 1review2010Protein Science
Toolkit/new switching mechanisms
new switching mechanisms
Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
New switching mechanisms are a protein engineering approach that introduces stimulus-responsive conformational switching into proteins that previously lacked such behavior. In the cited review, these engineered switches are described as enabling reagent-free biosensing and regulated biological function.
Usefulness & Problems
Why this is useful
This approach is useful because it expands switch-like behavior beyond naturally allosteric proteins to proteins that do not inherently undergo signaling-linked conformational change. The cited review positions such engineered switches as useful for biosensing and for controlling biological activity.
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 problem of how to convert non-switching proteins into molecules whose conformation and function respond to signaling events. This is presented as a route to create biosensors and regulated functional proteins from otherwise static binding proteins.
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
DerivedNew switching mechanisms are an engineering approach for introducing stimulus-responsive conformational changes into proteins that previously lacked such behavior. In the cited review context, these engineered switches are positioned as enabling biosensing and regulated biological function.
Taxonomy & Function
Primary hierarchy
Technique Branch
Method: A concrete method used to build, optimize, or evolve an engineered system.
Mechanisms
conformational 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 these switches arise through protein engineering and by joining proteins, consistent with domain fusion-based construct design. No specific cofactors, host expression systems, delivery methods, or sequence design rules are provided in the supplied evidence.
The supplied evidence is review-level and does not provide specific performance metrics, exemplar proteins, or quantitative validation for any one new switching mechanism. Although recombination is listed as a target process in the input, the provided evidence does not directly document a recombination-specific implementation.
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 new-switching-mechanisms
By ... formulating altogether new switching mechanisms, 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 review states that researchers can create switching properties by formulating new mechanisms rather than relying only on pre-existing natural allostery. The approach is specifically framed as supporting reagent-free biosensors and regulated biological functions.
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 co-opting natural allosteric coupling
new switching mechanisms and co-opting natural allosteric coupling 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 multiplexed engineering
new switching mechanisms 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 shRNA-delivered by lentivirus
new switching mechanisms 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.