Abstract
The unbinding force of Zif268-DNA complex has been studied by atomic force microscopy (AFM). DNA and Zif268 were covalently immobilized on the surfaces of an AFM tip and glass substrate, respectively. Confocal microscopy was used to confirm the successful immobilization of DNA. Because of the complexity of the protein-DNA interaction, parallel experiments were designed to discriminate specific interactions. For such experiments, a typical unbinding force of a single Zif268-DNA complex (approx 550 pN at 40 nN/s force loading rate) was evaluated.
Original language | English |
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Pages (from-to) | 87-93 |
Number of pages | 7 |
Journal | Nanobiotechnology |
Volume | 2 |
Issue number | 3-4 |
DOIs | |
State | Published - Sep 2006 |
Externally published | Yes |
Keywords
- AFM
- Force-distance curve
- Nonspecific interaction
- Protein-DNA complex
- Zif268-DNA unbinding force