Fig. 2: The free energy calculation of an individual phosphate group and fatty acid chains on a hKir6.2 tetramer. | Communications Chemistry

Fig. 2: The free energy calculation of an individual phosphate group and fatty acid chains on a hKir6.2 tetramer.

From: Evaluating inositol phospholipid interactions with inward rectifier potassium channels and characterising their role in disease

Fig. 2: The free energy calculation of an individual phosphate group and fatty acid chains on a hKir6.2 tetramer.

a Thermodynamic cycle used for the relative binding free energy calculations. The perturbation of the PIP2 headgroup (purple) was calculated in both the channel-bound state (ΔG2) and free in the PC membrane (grey rectangle (ΔG1)). ΔG3 and ΔG4 can be calculated using such methods as PMF calculations. b Coarse-grain to atomistic mapping of the phosphoniositides (PIP2, PI4P, PI, and PC). c Change in binding free energy (ΔΔG) when individual phosphate groups are perturbed (i.e., from PIP2 to PI4P, from PI4P to PI and from PI to PC (values in black). The sum of these free energy changes (i.e. from PIP2 to PC) is given in red. Values are rounded to the nearest whole number. d Change in binding free energy when PIP2 is perturbed to PC. Values are rounded to the nearest whole number. e Change in binding free energy when PIP2 is perturbed to PIP2-diC8. Values are rounded to the nearest whole number.

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