Abstract
Light scattering experiments were undertaken to study binding of the Max transcription factor to its E-box DNA recognition sequence. Translational diffusion coefficients were measured and the average hydrodynamic radii (Rh) of complexes calculated using the Stokes-Einstein equation. We detected both dimerization of Max and the formation of a stable complex with its E-box DNA target. These results demonstrate the applicability of Dynamic Light Scattering for measuring protein-DNA interactions.
Original language | English |
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Pages (from-to) | 199-203 |
Number of pages | 5 |
Journal | Cellular and Molecular Biology Letters |
Volume | 1 |
Issue number | 2 |
Publication status | Published - Jun 1996 |
Keywords
- Dynamic light scattering
- Max
- Protein-DNA interactions
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology