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https://www.selleckchem.com/products/sotrastaurin-aeb071.html Pyruvate metabolism requires the mitochondrial pyruvate carrier (MPC) proteins to transport pyruvate from the intermembrane space through the inner mitochondrial membrane to the mitochondrial matrix. The lack of the atomic structures of MPC hampers the understanding of the functional states of MPC and molecular interactions with the substrate or inhibitor. Here, we develop the de novo models of human MPC complexes and characterize the conformational dynamics of the MPC heterodimer formed by MPC1 and MPC2 (MPC1/2) by computational simulations. Our results reveal that functional MPC1/2 prefers to adopt an inward-open conformation, with the carrier open to the matrix side, whereas the outward-open states are less populated. The energy barrier for pyruvate transport in MPC1/2 is low enough, and the inhibitor UK5099 blocks the pyruvate transport by stably binding to MPC1/2. Notably, consistent with experimental results, the MPC1 L79H mutation significantly alters the conformations of MPC1/2 and thus fails for substrate transport. However, the MPC1 R97W mutation seems to retain the transport activity. The present de novo models of MPC complexes provide structural insights into the conformational states of MPC complexes and mechanistic understanding of interactions between the substrate/inhibitor and MPC proteins.A homemade instrument is designed to directly characterize the adhesion between two rigid polymeric microspheres in the presence of moist air. The tensile load is measured as a function of approach distance at designated relative humidity (RH). The measurement is consistent with our model from the first approximation. The model is further extended to include a rough surface. Capillary adhesion force is shown to be monotonically increasing with RH for smooth surfaces but becomes more pronounced at low RH for rough surfaces. Moisture has a profound influence on interparticle adhesion, which has significan

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