Source 1review2010Protein Science
Toolkit/protein conformational switch
protein conformational switch
Also known as: molecular switch
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
A protein conformational switch is an engineered protein system in which a signaling event induces a conformational change. Reported uses include reagent-free biosensing and regulation of biological function.
Usefulness & Problems
Why this is useful
This tool class is useful because it converts signaling events directly into protein structural changes, enabling reagent-free biosensors and proteins with regulated activity. The cited literature frames these switches as a way to endow proteins that previously lacked switching behavior with controllable responses.
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 creating proteins that respond to signaling inputs with a functional structural transition. This supports biosensing and functional regulation without requiring added reagents, according to the cited review.
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.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Techniques
Computational DesignTarget processes
signalingInput: Chemical
Implementation Constraints
The available evidence indicates that switching properties have been introduced into binding proteins by exploiting natural allosteric coupling, joining proteins, and creating new switching mechanisms. No specific construct architecture, cofactor requirement, expression system, or delivery method is described in the supplied evidence.
The provided evidence is high-level and does not specify particular protein scaffolds, ligands, dynamic range, kinetics, or validation assays. It also does not document a specific implementation, organism, or independent replication for any one switch design.
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.
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.
Approval Evidence
1 source2 linked approval claimsfirst-pass slug protein-conformational-switch
Proteins that switch conformations in response to a signaling event ... present a unique solution ... researchers are learning how to coax conformational changes from proteins that previously had none.
Source:
application scopesupports
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.
Source:
field challengesupports
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.
Source:
Comparisons
Source-backed strengths
The reported strength is conceptual versatility: engineered conformational switching can be applied both to biosensing and to regulation of biological function. The literature also indicates multiple engineering routes, including leveraging natural allosteric coupling, joining proteins, and creating new switching mechanisms.
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.
Ranked Citations
- 1.