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. Author manuscript; available in PMC: 2012 Jul 8.

Published in final edited form as: J Mol Biol. 2011 May 17;410(2):294–306. doi: 10.1016/j.jmb.2011.05.015

Heat evolved from the titration of ZnCl₂ into hIAPP_1–19 at pH 7.3 and 25°C, as measured by ITC. In solution with 100 mM Tris buffer and 100 μM NaCl ( ), zinc has one apparent binding site at sub- stoichiometric ratios of 0.136 zinc to 1 hIAPP_1–19. In the presence of 30% TFE ( ) the peptide adopts an α-helical conformation, causing a shift in the apparent binding stoichiometry of the primary binding site to 0.24 zinc to 1 hIAPP_1–19 and the addition of an endothermic process at higher concentrations of zinc.

Inline graphic — Heat evolved from the titration of ZnCl₂ into hIAPP_1–19 at pH 7.3 and 25°C, as measured by ITC. In solution with 100 mM Tris buffer and 100 μM NaCl ( ), zinc has one apparent binding site at sub- stoichiometric ratios of 0.136 zinc to 1 hIAPP_1–19. In the presence of 30% TFE ( ) the peptide adopts an α-helical conformation, causing a shift in the apparent binding stoichiometry of the primary binding site to 0.24 zinc to 1 hIAPP_1–19 and the addition of an endothermic process at higher concentrations of zinc.