Abstract
A modular adaptor consisting of a sequence-specific DNA binding zinc finger protein and a self-ligating protein-tag was developed to expedite efficient formation of a covalent linkage between an individual protein molecule and the programmed address modified with a tag-substrate on the DNA nanostructure.
| Original language | English |
|---|---|
| Journal | Chemical Communications |
| Volume | 51 |
| Issue number | 6 |
| Pages (from-to) | 1016-1019 |
| Number of pages | 4 |
| ISSN | 1359-7345 |
| DOIs | |
| Publication status | Published - 2015 |
| Externally published | Yes |
Keywords
- CHEMISTRY,
- NANOSTRUCTURES
- ORIGAMI
- NANOTECHNOLOGY
- REACTIVITY
- MOLECULES
- SCAFFOLDS
- COMPLEX
- Chemistry (all)
- Catalysis
- Ceramics and Composites
- Electronic, Optical and Magnetic Materials
- Surfaces, Coatings and Films
- Materials Chemistry
- Metals and Alloys
- Medicine (all)
- basic leucine zipper transcription factor
- DNA binding protein
- molecular scaffold
- oligodeoxynucleotide
- zinc finger protein
- DNA
- nanomaterial
- signal transducing adaptor protein
- Article
- binding kinetics
- binding site
- complex formation
- covalent bond
- crystal structure
- dissociation constant
- DNA binding
- DNA hybridization
- DNA protein complex
- DNA sequence
- environmental temperature
- hybridization
- in vitro study
- nucleotide sequence
- polyacrylamide gel electrophoresis
- protein DNA interaction
- static electricity
- atomic force microscopy
- chemistry
- metabolism
- Adaptor Proteins, Signal Transducing
- DNA-Binding Proteins
- Microscopy, Atomic Force
- Nanostructures
- Zinc Fingers
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