Hi. I am doing a protein that has hydrophobic interactions with itself. I want to test the effects of a peptide which is a truncated form of this protein. That means I need first to open the interactions of these proteins protein (dimer) while adding the peptide, then recover the hydrophobic interactions to check if the peptide can bind to the protein. I already check pH, salt, and temperature. None of them works. Does anybody know any good detergents and methods to achieve this? Thanks!!
Zoey Zheng
Proteins can be in the form of a spiral or a coil depending on the concentration. In addition, coils can appear due to hydrophobic interaction depending on the pH or concentration of the inorganic salt. If you dilute the protein dispersion with water again, i.e. reduce the concentration of the protein, it will again turn into a spiral. Hydrophobic interaction is an interaction mediated by water. What you are going to do from your question is not clear.
Sorry, I didn't make my point clear. This protein A can have hydrophobic interactions with another protein A in the cells through hydrophobic interactions. Therefore, we designed several peptides, which is the shorter form of protein A and hopefully, these peptides can block the interaction of protein A. We already expressed the Bifc-tagged protein A in the cells and got the cell lysates. Now we want to test the effects of these peptides in the cell lysates (Bifc-tagged protein A) to see if they can block such hydrophobic interactions.
We add the peptide into the Bifc-protein A cell lysates and test if pH, salt or different temperatures can open such interactions and therefore the peptide can bind with protein A once we neutralize it, lower the salt conc. or lower the temperature. But it seems either they can not open the interactions or they cannot recover the interactions (control without peptide).
Zoey Zheng
You need to click the consultant's last name, otherwise the robot does not send a letter to the consultant.
If you have two identical proteins interacting and you replace one of them with a shorter one, then you do not block the hydrophobic interaction, but only reduce the negative Gibbs energy of this interaction.
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