Fig. 3: Free energy calculations using disease-associated Kir6.2 mutations. | Communications Chemistry

Fig. 3: Free energy calculations using disease-associated Kir6.2 mutations.

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

Fig. 3: Free energy calculations using disease-associated Kir6.2 mutations.

a Schematic diagram showing the free energy calculation. An amino acid residue (blue spheres) is transformed into another residue (yellow spheres) between two states (PIP2 bound and free). b The energetic cost of making the residue mutation based on the schematic diagram (a).

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