Rod–Coil Block Copolymer: Fullerene Blend Water-Processable Nanoparticles: How Molecular Structure Addresses Morphology and Efficiency in NP-OPVs

The use of water-processable nanoparticles (WPNPs) is an emerging strategy for the processing of organic semiconducting materials into aqueous medium, dramatically reducing the use of chlorinated solvents and enabling the control of the nanomorphology in OPV active layers. We studied amphiphilic rod-coil block copolymers (BCPs) with a different chemical structure and length of the hydrophilic coil blocks. Using the BCPs blended with a fullerene acceptor material, we fabricated NP-OPV devices with a sustainable approach. The goal of this work is to clarify how the morphology of the nanodomains of the two active materials is addressed by the hydrophilic coil molecular structures, and in turn how the design of the materials affects the device performances. Exploiting a peculiar application of TEM, EFTEM microscopy on WPNPs, with the contribution of AFM and spectroscopic techniques, we correlate the coil structure with the device performances, demonstrating the pivotal influence of the chemical design over material properties. BCP5, bearing a coil block of five repeating units of 4-vinilpyridine (4VP), leads to working devices with efficiency comparable to the solution-processed ones for the multiple PCBM-rich cores morphology displayed by the blend WPNPs. Otherwise, BCP2 and BCP15, with 2 and 15 repeating units of 4VP, respectively, show a single large PCBM-rich core; the insertion of styrene units into the coil block of BCP100 is detrimental for the device efficiency, even if it produces an intermixed structure.

Structural Effects of Disease-Related Mutations in Actin-Binding Period 3 of Tropomyosin

Tropomyosin (Tpm) is an actin-binding coiled-coil protein. In muscle, it regulates contractions in a troponin/Ca2+-dependent manner and controls the thin filament lengths at the pointed end. Due to its size and periodic structure, it is difficult to observe small local structural changes in the coiled coil caused by disease-related mutations. In this study, we designed 97-residue peptides, Tpm1.164–154 and Tpm3.1265–155, focusing on the actin-binding period 3 of two muscle isoforms. Using these peptides, we evaluated the effects of cardiomyopathy mutations: I92T and V95A in Tpm1.1, and congenital myopathy mutations R91P and R91C in Tpm3.12. We introduced a cysteine at the N-terminus of each fragment to promote the formation of the coiled-coil structure by disulfide bonds. Dimerization of the designed peptides was confirmed by gel electrophoresis in the presence and absence of dithiothreitol. Using circular dichroism, we showed that all mutations decreased coiled coil stability, with Tpm3.1265–155R91P and Tpm1.164–154I92T having the most drastic effects. Our experiments also indicated that adding the N-terminal cysteine increased coiled coil stability demonstrating that our design can serve as an effective tool in studying the coiled-coil fragments of various proteins.

Optimization of a Two-Layer 3D Coil Structure with Uniform Magnetic Field

Conventional magnetically coupled resonant wireless power transfer systems are faced with resonant frequency splitting phenomena and impedance mismatch when a receiving coil is placed at misaligned position. These problems can be avoided by using uniform magnetic field distribution at receiving plane. In this paper, a novel 3D transmitting coil structure with improved uniform magnetic field distribution is proposed based on a developed optimization method. The goal is to maximize the average magnetic field strength and uniform magnetic field section of the receiving plane. Hence, figures of merit (FoM1 and FoM2) are introduced and defined as product of average magnetic field strength and length or surface along which uniform magnetic field is generated, respectively. The validity of the optimization method is verified through laboratory measurements performed on the fabricated coils driven by signal generator at operating frequency of 150 kHz. Depending on the allowed ripple value and predefined coil proportions, the proposed transmitting coil structure gives the uniform magnetic field distribution across 50% to 90% of the receiving plane.

Research on Coil Identification Algorithm of Wireless Power Transfer System Based on Magnetic Field Features

In the practical application of wireless power transfer (WPT), the identification of the secondary coil and the analysis of the space magnetic field of the coil will affect the matching scheme of the coil, which will further affect the performance of energy transmission. At present, the establishment of the coil space magnetic field model mainly adopts the finite element method (FEM). The accuracy of the results is limited by the computer performance and the specific settings during calculation, which usually takes a long time. Additionally, it can only analyze and establish the space magnetic field of the coil with specific parameters. Especially when the coil structure and parameters change, it is difficult to quickly establish the spatial magnetic field. This paper presents a secondary side coil identification method of a wireless charging system based on the magnetic field cloud image characteristics. The image feature extraction algorithm is used to extract features of a certain height magnetic field cloud image of an unknown structure type coil obtained by FEM. Further, by matching with the characteristics of the magnetic field cloud image of the known coil, the identification of the unknown coil structure type is realized. The effectiveness and accuracy of the proposed method is verified by an example. This algorithm is helpful to extract the characteristics of the coil space magnetic field, and can establish coil space magnetic field models with different structure types and different coil parameters combined with deep learning to guide the matching scheme of the primary and secondary coils, and realize efficient energy transmission.

A New Strategy for the Preparation of Porous Silk Fibroin Scaffolds

In order to prepare Silk Fibroin (SF) scaffolds with excellent pore structure, the fresh SF solution was concentrated at relative humidity 55% and 25°C for 3 days. During the above process, SF micelles, existed in the fresh SF solution, aggregated into nanofilaments as concentration increased, and the nanofilament feature of SF were similar to that observed in silk gland. SF nanofilaments were easy to form SF scaffolds with porous and silk I structure, in contrary, SF micelles were liable for formation of SF scaffolds with lamellar and random coil structure. It suggested that the formation of SF nanofilaments is a critical step for pore and secondary structure control of lyophilized SF scaffolds.

A Novel Planar Differential Koch Fractal Eddy Current Probe with Parallel Wound Topological Structure

Flexible planar eddy current probes are widely used to detect conductive components with complex surface. In this study, topological transformation is applied to design a differential Koch coil exciting eddy current probe. Two kinds of Koch exciting coils, Koch A and Koch B , were obtained by topological transformation from a three-dimensional differential exciting eddy current probe. Finite element model simulation is conducted to visualize the differences of eddy current distributions induced by the probes and get the defect signal. A detailed comparison is made among the two kinds of Koch eddy current probes and a circular eddy current probe by experiments. The experiments demonstrate that the sensitivity of the Koch A eddy current probe is higher than that of another two probes for detecting the defect which is shorter than the size of the probe. This work provides a novel method for improving the performance of eddy current probes in the coil structure design.

Control of the serine integrase reaction: roles of the coiled-coil and helix E regions in DNA site synapsis and recombination

Bacteriophage serine integrases catalyze highly specific recombination reactions between defined DNA segments called att sites. These reactions are reversible depending upon the presence of a second phage-encoded directionality factor. The bipartite C-terminal DNA binding region of integrases includes a recombinase domain (RD) connected to a zinc-binding domain (ZD), which contains a long flexible coiled-coil (CC) motif that extends away from the bound DNA. We directly show that the identities of the phage A118 integrase att sites are specified by the DNA spacing between the RD and ZD DNA recognition determinants, which in turn, directs the relative trajectories of the CC motifs on each subunit of the att -bound integrase dimer. Recombination between compatible dimer-bound att sites requires minimal length CC motifs and 14 residues surrounding the tip where pairing of CC motifs between synapsing dimers occurs. Our alanine-scanning data suggests that molecular interactions between CC motif tips may differ in integrative ( attP x attB ) and excisive ( attL x attR ) recombination reactions. We identify mutations in 5 residues within the integrase oligomerization helix that control the remodeling of dimers into tetramers during synaptic complex formation. Whereas most of these gain-of-function mutants still require the CC motifs for synapsis, one mutant efficiently, but indiscriminantly, forms synaptic complexes without the CC motifs. However, the CC motifs are still required for recombination, suggesting a function for the CC motifs after initial assembly of the integrase synaptic tetramer. Importance The robust and exquisitely-regulated site-specific recombination reactions promoted by serine integrases are integral to the life cycle of temperate bacteriophage, and in the case of the A118 prophage, are an important virulence factor by Listeria monocytogenes . The properties of these recombinases have led to their repurposing into tools for genetic engineering and synthetic biology. In this report, we identify determinants regulating synaptic complex formation between correct DNA sites, including the DNA architecture responsible for specifying the identity of recombination sites, features of the unique coiled-coil structure on the integrase that are required to initiate synapsis, and amino acid residues on the integrase oligomerization helix that control the remodeling of synapsing dimers into a tetramer active for DNA strand exchange.