The oligomerization of protein macromolecules on cell membranes plays a fundamental role in regulating cellular function. From modulating signal transduction to directing immune response, membrane proteins (MPs) play a crucial role in biological processes and are often the target of many pharmaceutical drugs. Despite their biological relevance, the challenges in experimental determination have hampered the structural availability of membrane proteins and their complexes.
View Article and Find Full Text PDFTwo mononuclear iron(II) complexes, [(6-amide-BPMEN)Fe](OTf) () and [(6-amide-Me-BPMEN)Fe(OTf)](OTf) (), supported by two BPMEN-derived (BPMEN = ,-dimethyl-,-bis(pyridine-2-yl-methyl)ethane-1,2-diamine) ligands bearing one or two amide functionalities have been isolated to study their reactivity in the oxygenation of C-H and C═C bonds using isopropyl 2-iodoxybenzoate (Pr-IBX ester) as the oxidant. Both and contain six-coordinate high-spin iron(II) centers in the solid state and in solution. The 6-amide-BPMEN ligand stabilizes an = 1 iron(IV)-oxo intermediate, [(6-amide-BPMEN)Fe(O)] ().
View Article and Find Full Text PDFSurface features' morphology is crucial in designing lubricant-infused slippery surfaces (LIS). Microcavities were hypothesized to provide lower physical pinning, reduced droplet normal adhesion, and superior lubricant retention as compared to micropillars and untextured surfaces. Micropillars and microcavities ( = 10 ± 3 μm, = 8 ± 1 μm, = 17 ± 3 μm, = 1.
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