Variational calculations for resonance oscillations of inhomogeneous plasmas

The electrostatic resonance properties of an inhomogeneous plasma column are reported by application of the Rayleigh-Ritz method. A description of the rf equation of motion and pressure term that expresses the system of equations in Euler-Lagrange form is presented. The Rayleigh-Ritz procedure is applied to the corresponding Lagrangian to obtain approximate resonance frequencies and eigenfunctions. An appropriate set of trial coordinate functions is defined, which leads to frequency and eigenfunction estimates

A low-bandgap dimeric porphyrin molecule for 10% efficiency solar cells with small photon energy loss

Dimeric porphyrin molecules have great potential as donor materials for high performance bulk heterojunction organic solar cells (OSCs). Recently reported dimeric porphyrins bridged by ethynylenes showed power conversion efficiencies (PCEs) of more than 8%. In this study, we design and synthesize a new conjugated dimeric D-A porphyrin ZnP2BT-RH, in which the two porphyrin units are linked by an electron accepting benzothiadiazole (BT) unit. The introduction of the BT unit enhances the electron delocalization, resulting in a lower highest occupied molecular orbital (HOMO) energy level and an increased molar extinction coefficient in the near-infrared (NIR) region. The bulk heterojunction solar cells with ZnP2BT-RH as the donor material exhibit a high PCE of up to 10% with a low energy loss (Eloss) of only 0.56 eV. The 10% PCE is the highest for porphyrin-based OSCs with a conventional structure, and this Eloss is also the smallest among those reported for small molecule-based OSCs with a PCE higher than 10% to date

Helix vs. Sheet Formation in a Small Peptide

Segments with the amino acid sequence EKAYLRT appear in natural occurring proteins both in $\alpha$-helices and $\beta$-sheets. For this reason, we have use this peptide to study how secondary structure formation in proteins depends on the local environment. Our data rely on multicanonical Monte Carlo simulations where the interactions among all atoms are taken into account. Results in gas phase are compared with that in an implicit solvent. We find that both in gas phase and solvated EKAYLRT forms an $\alpha$-helix when not interacting with other molecules. However, in the vicinity of a $\beta$-strand, the peptide forms a $\beta$-strand. Because of this change in secondary structure our peptide may provide a simple model for the $\alpha \to \beta$ transition that is supposedly related to the outbreak of Prion diseases and similar illnesses.Comment: to appear in Physical Review