Speaker
Description
Here we demonstrate preliminary results on the structural studies of human pre-Haptoglobin-2. We have established protocols to recombinantly produce pre-haptoglobin-2 and biophysically characterised it using various methods. Recombinant pre-haptoglobin-2 and its glycosylation sites have been verified by MS. Furthermore, Small-Angle X-rays Scattering (SAXS) has been employed for acquiring a low resolution structural model of the protein and its oligomeric assembly. We have produced mutants that do not process further to mature haptoglobin as well as mutants that cannot form higher oligomers. The aforementioned mutants lacking the ability to form higher oligomers have been performed in varied crystallization trials whereas no crystals have been obtained.
