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. Author manuscript; available in PMC: 2010 Feb 26.
Published in final edited form as: J Phys Chem B. 2009 Feb 26;113(8):2498–2505. doi: 10.1021/jp810261x

Figure 2.

Figure 2

Intensities in anti-symmetric β-sheet and “random coil” regions versus aggregation time for (a) uncatalyzed and (b) membrane-catalyzed hIAPP folding. The dashed line indicates at t=14 minutes lipid vesicles were added. Intensities are normalized to minimum and maximum of individual kinetic traces. (c) Normalized intensities of anti-symmetric β-sheet feature for uncatalyzed (green) and catalyzed (blue). (d) Intensities in “random coil” region (1642 cm-1), for the (green) uncatalyzed, (blue) catalyzed hIAPP experiment and (red) rIAPP experiment. Intensities are normalized to starting values at t= 0.