Matthewssilva5933

The development of three-dimensional aperiodic energy storage devices is in part impeded by the lack of appropriate aperiodic templates that can withstand the thermal conditions required to deposit energy storage materials within their void space. Herein, the feasibility of an aperiodic three-dimensional architecture for energy storage is demonstrated for the first time by constructing a tricontinuous conductor-insulator-conductor (CIC) nanocapacitor on an aperiodic nanoporous gold scaffold. To accomplish this, the scaffold was characterized using in situ small-angle X-ray scattering (SAXS) during exposure to a thermal environment, revealing that its microstructure eventually stabilizes after undergoing a phase of rapid coarsening, indicating a departure from the 1/4 time-dependent power-law coarsening behavior usually observed at the early stage of the coarsening process. Using this stability regime, we created the CIC by intentionally precoarsening and stabilizing the scaffold before depositing two dissimilar metal oxide films in its void space by atomic layer deposition. Current-voltage characteristics and electrochemical impedance spectroscopy measurements revealed that the un-optimized 3D CIC outperformed its 2D counterpart by ∼4× in terms of capacitance. This proof-of-concept device will pave the way to the development of aperiodic three-dimensional energy storage systems with enhanced energy and power densities.The CETSA and Thermal Proteome Profiling (TPP) analytical methods are invaluable for the study of protein-ligand interactions and protein stability in a cellular context. These tools have increasingly been leveraged in work ranging from understanding signaling paradigms to drug discovery. Consequently, there is an important need to optimize the data analysis pipeline that is used to calculate protein melt temperatures (Tm) and relative melt shifts from proteomics abundance data. Here, we report a user-friendly analysis of the melt shift calculation workflow where we describe the impact of each individual calculation step on the final output list of stabilized and destabilized proteins. This report also includes a description of how key steps in the analysis workflow quantitatively impact the list of stabilized/destabilized proteins from an experiment. We applied our findings to develop a more optimized analysis workflow that illustrates the dramatic sensitivity of chosen calculation steps on the final list of reported proteins of interest in a study and have made the R based program Inflect available for research community use through the CRAN repository [McCracken, N. Inflect Melt Curve Fitting and Melt Shift Analysis. R package version 1.0.3, 2021]. The Inflect outputs include melt curves for each protein which passes filtering criteria in addition to a data matrix which is directly compatible with downstream packages such as UpsetR for replicate comparisons and identification of biologically relevant changes. Overall, this work provides an essential resource for scientists as they analyze data from TPP and CETSA experiments and implement their own analysis pipelines geared toward specific applications.The thiamin diphosphate-dependent enzyme 1-deoxy-d-xylulose 5-phosphate synthase (DXPS) catalyzes the formation of DXP from pyruvate (donor) and d-glyceraldehyde 3-phosphate (d-GAP, acceptor). DXPS is essential in bacteria but absent in human metabolism, highlighting it as a potential antibacterial drug target. BMS493 The enzyme possesses unique structural and mechanistic features that enable development of selective inhibition strategies and raise interesting questions about DXPS function in bacterial pathogens. DXPS distinguishes itself within the ThDP enzyme class by its exceptionally large active site and random sequential mechanism in DXP formation. In addition, DXPS displays catalytic promiscuity and relaxed acceptor substrate specificity, yet previous studies have suggested a preference for pyruvate as the donor substrate when d-GAP is the acceptor substrate. However, such donor specificity studies are potentially hindered by a lack of knowledge about specific, alternative donor-acceptor pairs. In this study, we exploited the promiscuous oxygenase activity of DXPS to uncover alternative donor substrates for DXPS. Characterization of glycolaldehyde, hydroxypyruvate, and ketobutyrate as donor substrates revealed differences in stabilization of enzyme-bound intermediates and acceptor substrate usage, illustrating the influence of the donor substrate on reaction mechanism and acceptor specificity. In addition, we found that DXPS prevents abortive acetyl-ThDP formation from a DHEThDP carbanion/enamine intermediate, similar to transketolase, supporting the potential physiological relevance of this intermediate on DXPS. Taken together, these results offer clues toward alternative roles for DXPS in bacterial pathogen metabolism.Bimetallic nanoparticles (NPs) are complex systems with properties that far exceed those of the individual constituents. In particular, association of a noble metal and a first-row transition metal are attracting increasing interest for applications in catalysis, electrocatalysis, and magnetism, among others. Such objects display a rich structural chemistry thanks to their ability to form intermetallic phases, random alloys, or core-shell species. However, under reaction conditions, the surface of these nanostructures may be modified due to migration, segregation, or isolation of single atoms, leading to the formation of original structures with enhanced catalytic activity. In this respect, Zakhtser et al. report in this issue of ACS Nano the synthesis and study of the chemical evolution of the surface of a series of PtZn nanostructured alloys. In this Perspective, we report some selected examples of bimetallic nanocatalysts and their increased activity compared to that of the corresponding pure noble metal, with a special focus on Pt-based systems. We also discuss the mobility of the species present on the catalyst surface and the electronic influence of one metal to the other.The nature of anionic alkali metals in solution is traditionally thought to be "gaslike" and unperturbed. In contrast to this noninteracting picture, we present experimental and computational data herein that support ion pairing in alkalide solutions. Concentration dependent ionic conductivity, dielectric spectroscopy, and neutron scattering results are consistent with the presence of superalkali-alkalide ion pairs in solution, whose stability and properties have been further investigated by DFT calculations. Our temperature dependent alkali metal NMR measurements reveal that the dynamics of the alkalide species is both reversible and thermally activated suggesting a complicated exchange process for the ion paired species. The results of this study go beyond a picture of alkalides being a "gaslike" anion in solution and highlight the significance of the interaction of the alkalide with its complex countercation (superalkali).