Toolkit/circular permutation
circular permutation
Also known as: CP
Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Circular permutation (CP) is an invaluable approach to redesigning a protein by rearranging the amino acid sequence, where the connectivity of the secondary structural elements is altered without changing the overall structure of the protein.
Usefulness & Problems
No literature-backed usefulness or problem-fit explainer has been materialized for this record yet.
Taxonomy & Function
Primary hierarchy
Technique Branch
Method: A concrete method used to build, optimize, or evolve an engineered system.
Target processes
editingInput: Light
Validation
Supporting Sources
Ranked Claims
Artificial circularly permuted proteins are used in biocatalysis, fluorescence-based small-molecule sensing, genome editing, ligand-binding protein switches, and optogenetic engineering.
Circular permutation redesigns a protein by rearranging amino acid sequence connectivity of secondary-structure elements without changing the overall protein structure.
Circular permutation can lead to either reduced or enhanced protein stability or catalytic efficiency.
The effects of circular permutation on a protein's energy landscape cannot be predicted a priori.
Approval Evidence
Circular permutation (CP) is an invaluable approach to redesigning a protein by rearranging the amino acid sequence, where the connectivity of the secondary structural elements is altered without changing the overall structure of the protein.
Source:
Artificial circularly permuted proteins are used in biocatalysis, fluorescence-based small-molecule sensing, genome editing, ligand-binding protein switches, and optogenetic engineering.
Source:
Circular permutation redesigns a protein by rearranging amino acid sequence connectivity of secondary-structure elements without changing the overall protein structure.
Source:
Circular permutation can lead to either reduced or enhanced protein stability or catalytic efficiency.
Source:
The effects of circular permutation on a protein's energy landscape cannot be predicted a priori.
Source:
Comparisons
No literature-backed comparison notes have been materialized for this record yet.
Ranked Citations
- 1.