Protein unfolding can lead to aggregation and is linked to protein conformational disorders. In order to learn more about the effect of hydrodynamic forces on protein unfolding Dave Dunstan and co-workers at University of South Australia and The University of Melbourne, Australia, have studied the unfolding of polypeptide helices under shear flow using real-time circular dichroism.
The extent of unfolding is dependent on the monomer size of the poly-L-lysine chains, as well as shear rate and the duration of its application. The shear-stability of the α-helical poly-L-lysine structure increased with increasing chain-length.
Interested to know more? Read the full article for free here:
Don’t forget you can also keep up-to-date with all the latest news from Soft Matter on Twitter!
