Misfolding and amyloid fibril formation by human islet amyloid polypeptide (hIAPP) are
thought to be important in the pathogenesis of type 2 diabetes, but the structures of the
misfolded forms remain poorly understood. Here we developed an approach that combines
site-directed spin labeling with continuous wave and pulsed EPR to investigate local
secondary structure and to determine the relative orientation of the secondary structure
elements with respect to each other. These data indicated that individual hIAPP molecules …