Impact of charge switching stimuli on supramolecular perylene monoimide assemblies
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The introduced two-dimensional representation of two-parameter signal dependence allows for clear interpretation and classification of the measured signal upon using machine learning methods.
Mg 2+ electroplating has been an obstacle for Mg metal batteries due to the passivating nature of Mg metal. Here, a unique current collector based on an amorphous MgO-wrapped Zn-skeleton enabled Mg 2+ electroplating for a high-voltage Mg metal battery.
Trypanosoma brucei PRMT7 (TbPRMT7) is a protein arginine methyltransferase (PRMT) that strictly monomethylates various substrates, thus classifying it as a type III PRMT. However, the molecular basis of its unique product specificity has remained elusive. Here, we present the structure of TbPRMT7 in complex with its cofactor product S-adenosyl-L-homocysteine (AdoHcy) at 2.8 Å resolution and identify a glutamate residue critical for its monomethylation behavior. TbPRMT7 comprises the conserved methyltransferase and β-barrel domains, an N-terminal extension, and a dimerization arm. The active site at the interface of the N-terminal extension, methyltransferase, and β-barrel domains is stabilized by the dimerization arm of the neighboring protomer, providing a structural basis for dimerization as a prerequisite for catalytic activity. Mutagenesis of active-site residues highlights the importance of Glu181, the second of the two invariant glutamate residues of the double E loop that coordinate the target arginine in substrate peptides/proteins and that increase its nucleophilicity. Strikingly, mutation of Glu181 to aspartate converts TbPRMT7 into a type I PRMT, producing asymmetric dimethylarginine (ADMA). Isothermal titration calorimetry (ITC) using a histone H4 peptide showed that the Glu181Asp mutant has markedly increased affinity for monomethylated peptide with respect to the WT, suggesting that the enlarged active site can favorably accommodate monomethylated peptide and provide sufficient space for ADMA formation. In conclusion, these findings yield valuable insights into the product specificity and the catalytic mechanism of protein arginine methyltransferases and have important implications for the rational (re)design of PRMTs.
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Gallium oxide is an emerging wide band-gap material that has the potential to penetrate the power electronics market in the near future. In this paper, a finite-element gallium oxide semiconductor model is presented that can predict the electrical and thermal characteristics of the device. The finite element model of the two-dimensional device architecture is developed inside the Sentaurus environment. A vertical FinFET device architecture is employed to assess the device's behavior and its static and dynamic behavior. Enhancement-mode device operation is realized with this type of device architecture without the need for any selective area doping. The dynamic thermal behavior of the device is characterized through its short-circuit behavior. Based on the device static and dynamic behavior, it is envisioned that reliable vertical transistors can be fabricated for the power electronics applications.
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An apparatus for switch wear leveling includes a switching module that controls switching for two or more pairs of switches in a switching power converter. The switching module controls switches based on a duty cycle control technique and closes and opens each switch in a switching sequence. The pairs of switches connect to a positive and negative terminal of a DC voltage source. For a first switching sequence a first switch of a pair of switches has a higher switching power loss than a second switch of the pair of switches. The apparatus includes a switch rotation module that changes the switching sequence of the two or more pairs of switches from the first switching sequence to a second switching sequence. The second switch of a pair of switches has a higher switching power loss than the first switch of the pair of switches during the second switching sequence.