Hy everyone,
i want to analyze the binding of a protein to mutlilamellar vesicles (MLVs). My problem is, that the protein I'm using tends to form multimers or aggregates and to avoid this we thought about adding Tween-20 to the protein solution. However, this might interfere with the stability of the MLVs. Can anyone give me information on the concentration of Tween-20 I can use in the presence of MLVs without disturbing their structure?
Or do you think adding Tween-20 won't help in creating monomers?
All the best,
Pascal
I am so sorry, but there is just so much wrong in this project.
Your protein, multimer, aggregate, whatever is loaded with tween-20 detergent and you are looking to see how it interacts with lipid vesicles.
Solubilizing aggregated protein using tween-20 (which has a Critical micelle concentration (CMC) of ~0,1 mM) and expecting meaningful data when interacts with mutlilamellar vesicles is just wrong.
Isn't there anybody at the Leibniz Institute that can help you out with this?
Thank you for your answer.
To check if I understood you correct:
So you say that the protein will be loaded with tween-20? This would then lead to an improved incorporation of the protein into the membrane, right?
If that's the case, then I agree that it's nonsense.
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