Very nice to finally have this work out too. Another great collaboration with Prof. Molinari in Milan, here we demonstrate the strategic role of a Phe16 (or equivalent) for the folding of transaminases. We found a native TA which had a threonine at that position and was expressed only insolubly. By replacing the T for a P we generated a soluble protein which could be fully characterised.

Well done Benni!

Read the full paper here

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