Hallo everyone!
Need an advice, in an experimental setup. In brief, I study a protein which undergoes a proteolytic processing. It is known that the protein is present upon physiological expression as a dimer, and also can form multimers. What is not known about this protein: whether the proteolysis goes before or after the dimerization (or multimerization).
I can produce the recombinant protein and it forms dimers, and the dimers contain the processed form - all as expected.
But how can I setup an experiment to check, if the proteolysis require the dimerization in advance, or just a monomer can be efficiently processed?
You would need a method to prevent dimerization. By studying the dimer interface, you might be able to work out what site-directed mutations could be made to block its formation while still allowing the protein to fold properly. For example, introduce a bulky amino acid side chain where a small side chain would normally be important at the dimer interface.
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