Skip to main content
. Author manuscript; available in PMC: 2014 Jun 2.
Published in final edited form as: Phys Chem Chem Phys. 2013 Aug 14;15(30):12558–12571. doi: 10.1039/c3cp44542a

Fig. 4.

Fig. 4

Cu2+ inhibits human amylin secondary conformational transitions in solution. (A–D) Comparative far-UV CD data for the conformational changes of human amylin (20 μM) in PBS alone or in the presence of equimolar amount of Cu2+. In the presence of Cu2+, human amylin conformational transitions to a β-sheet-rich structure are blocked.