Quad-Band Metamaterial Perfect Absorber with High Shielding Effectiveness Using Double X-Shaped Ring Resonator.

This study assesses quad-band metamaterial perfect absorbers (MPAs) based on a double X-shaped ring resonator for electromagnetic interference (EMI) shielding applications. EMI shielding applications are primarily concerned with the shielding effectiveness values where the resonance is uniformly or non-sequentially modulated depending on the reflection and absorption behaviour. The proposed unit cell consists of double X-shaped ring resonators, a dielectric substrate of Rogers RT5870 with 1.

An Ultra-Thin, Triple-Band, Incident Angle-Insensitive Perfect Metamaterial Absorber.

We created an ultra-thin, triple-band incident angle-insensitive perfect metamaterial absorber (MMA) with a metallic patch and a continuous metal ground isolated by a central dielectric substrate. The top metallic patch, placed across the edges of the 0.58 mm thickness Rogers RO4003C (lossy) substrate, forms the bulk of the projected absorber's ultra-thin layer.

Selenite uptake by outer membrane porin ExtI and its involvement in the subcellular localization of rhodanese-like lipoprotein ExtH in Geobacter sulfurreducens.

Selenite reduction is a key step in the biogeochemical cycle of selenium-an essential trace element for life. A variety of bacteria can transform selenite into elemental selenium nanoparticles on the cell surface via anaerobic respiration or detoxification processes. However, the proteins associated with the uptake of selenite for these processes are poorly understood.

Characterization of a Novel Porin-Like Protein, ExtI, from Geobacter sulfurreducens and Its Implication in the Reduction of Selenite and Tellurite.

The gene in encodes a putative outer membrane channel porin, which resides within a cluster of genes. This cluster is highly conserved across the and includes multiple putative -type cytochromes. In silico analyses of the ExtI sequence, together with Western blot analysis and proteinase protection assays, showed that it is an outer membrane protein.