I am doing a DNA-protein binding kinetics experiment, and I would like to ask your expertise regarding factors that affect DNA-protein interactions such as salt, cofactors, etc.
I agree with Ross Thomson! There are several factors that can affect the binding of protein to DNA.
If you are interested to measure the affinity of protein-DNA interactions at different conditions (different salt concentrations, different pH, etc.), I would suggest to perform MicroScale Thermophoresis (MST) experiments. MST allows you to measure binding affinities in all kind of buffers, even in serum and cell lysate. So you will be able to find optimal conditions and you will be able to determine parameters that are absolutely crucial and some others that your binding can tolerate more.
For more information, you can read this review or visit our website:
http://www.nanotemper-technologies.com/news-events/news/article/microscale-thermophoresis-more-than-binding-affinities/
http://www.nanotemper-technologies.com//home/
Thank you Heide Marie Roth. I just know about what you mentioned now. It is a good advise from you. Sincerely,
Protein-DNA interactions are controlled by different factors such as DNA sequencing and shape, hydrogen bonds, and van der Waals forces of attraction.
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