Abstract
Membrane-integral pyrophosphatases (mPPases) are clinically relevant enzymes responsible for the breakdown of inorganic pyrophosphate and translocating a cation across the membrane. Recent mechanistic developments led to the hypothesis that the protein environment may be important for function and intersubunit communication. In this study, molecular dynamics simulations at the coarse-grained and atomistic resolution of the mPPase from Thermotoga maritima (Tm-PPase) with varying lipid bilayer components were assembled and simulated.
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