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. Author manuscript; available in PMC: 2018 Nov 5.
Published in final edited form as: Comput Chem Eng. 2018 Feb 21;116:322–332. doi: 10.1016/j.compchemeng.2018.02.013

Fig. 2.

Fig. 2

Free energy landscape (FEL) constructed from the 2D probability of principal components PC1 and PC2, calculated for the modeled region of the HI18:IAPP complex (residues 9 through 12 of HI18, subunit 1 and residues 1 through 9 of IAPP) derived from REMD simulations at 300 K. The global free energy minimum of the FEL is encircled in a black oval shape. Within the free energy minimum basin, the structures encompass a salt-bridge between subunit 1 residue Glu10 of HI18 with primarily the positively charged N-terminal domain of residues Lys1 of IAPP and, in a few structures, the side chain group of the same IAPP residue. The representative structure which was extracted from the FEL and used as a template and initial structure for the subsequent MD simulations is shown at the bottom of the FEL.