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. 2014 Nov 20;10(11):e1003987. doi: 10.1371/journal.pcbi.1003987

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© 2014 Äijänen et al

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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A) Secondary structure of helix X (residues 461–472) during simulations L1 and L2. B) Simulation snapshots from simulations L1 and L2. Helix X is colored to highlight the changes in the secondary structure. In the absence of anacetrapib (L1), helix X maintains the α-helical structure, whereas in the presence of anacetrapib (L2) it alternates between turn (unfolding of the helix) and 3₁₀-helix (extension of the helix). Turn-like conformation is presented in the figure.