Nowadays, there are still countless researchers defending the effectiveness of the moving average technical analysis and they are able to present evidences for certain stocks, indexes and/or markets where this technical indicator is extremely useful for defining trading strategies. But the contrary also exists, i.e. a lot of researchers show distrust of this technical indicator and also provide evidences with particular stocks, indexes and/or markets where moving averages based strategies do not work well.
Aiming to understand why is it that with some stocks the moving average is indeed an excellent indicator while with others it is not, in this paper we implement moving average based strategies to buy and/or sell stocks for more than 480 companies from the NASDAQ 100, FTSE 100 and SP 500 indexes and compare the results with the ones obtained when using the buy-and-hold strategy.

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TheBacteroides thetaiotaomicronhas developed a consortium of enzymes capable of overcoming steric constraints and degrading, in a sequential manner, the complex rhamnogalacturonan II (RG-II) polysaccharide. BT0996 protein acts in the initial stages of the RGII depolymerisation, where its two catalytic modules remove the terminal monosaccharides from RG-II side chains A and B. BT0996 is modular and has three putative carbohydrate-binding modules (CBMs) for which the roles in the RG-II degradation are unknown. Here, we present the characterisation of themoduleat the C-terminal domain, which we designated BT0996C. The high-resolution structure obtained by X-ray crystallography reveals that the protein displays a typical β-sandwich fold with structural similarity to CBMs assigned to families 6 and 35. The distinctive features are: 1) the presence of several charged residues at the BT0996-C surface creating a large, broad positive lysine-rich patch that encompasses the putative binding site; and 2) the absence of the highly conserved binding-site signatures observed in CBMs from families 6 and 35, such as region A tryptophan and region C asparagine. These findings hint at a binding mode of BT0996-C not yet observed in its homologues. In line with this, carbohydrate microarrays and microscale thermophoresis show the ability of BT0996-C to bind α1-4-linked polygalacturonic acid, and that electrostatic interactions are essential for the recognition of the anionic polysaccharide. The results support the hypothesis that BT0996-C may have evolved to potentiate the action of BT0996 catalytic modules on the complex structure of RG-II by binding to the polygalacturonic acid backbone sequence.

Ostriches are known to be the fastest bipedal animal alive; to accomplish such an achievement, their anatomy evolved to sustain the stresses imposed by running at such velocities. Ostriches represent an excellent case study due to the fact that their locomotor kinematics have been extensively studied for their running capabilities. The shape and structure of ostrich bones are also known to be optimized to sustain the stresses imposed by the body mass and accelerations to which the bones are subjected during movements. This study focuses on the limb bones, investigating the structure of the bones as well as the material properties, and how both the structure and material evolved to maximise the performance while minimising the stresses applied to the bones themselves. The femoral shaft is hollowed and it presents an imbricate structure of fused bone ridges connected to the walls of the marrow cavity, while the tibial shaft is subdivided into regions having different mechanical characteristics. These adaptations indicate the optimization of both the structure and the material to bear the stresses. The regionalization of the material highlighted by the mechanical tests represents the capability of the bone to adapt to external stimuli during the life of an individual, optimizing not only the structure of the bone but the material itself.

This paper presents a pulse amplitude modulated signal generator to address inference in Memristor based Neural Network Accelerators. As a part of this system, a novel 8-bit capacitive segmented Digital to Analog Converter (DAC) using amorphous Indium Galium Zinc Oxide (a-IGZO) thin-film transistor (TFT) technology has been designed. The DAC employs 50% segmentation with binary coded least significant bits (LSBs) and unary coded most significant bits (MSBs). This circuit has shown an ENOB of 7.3 bits at a sampling frequency of 100 kHz and an input frequency of 50 kHz. The worst case INL and DNL were recorded as 0.047 LSB and 0.34 LSB, respectively. With a power supply voltage of 5 V for the operational amplifier and 3V as the DAC reference voltage, the power consumption of the complete DAC was around 1.25 mW. This circuit can find potential applications in different flexible electronics systems.

Neisseria gonorrhoeae is an obligate human pathogenic bacterium responsible for gonorrhea, a sexually transmitted disease. The bacterial peroxidase, an enzyme present in the periplasm of this bacterium, detoxifies the cells against hydrogen peroxide and constitutes one of the primary defenses against exogenous and endogenous oxidative stress in this organism. The 38 kDa heterologously produced bacterial peroxidase was crystallized in the mixed-valence state, the active state, at pH 6.0, and the crystals were soaked with azide, producing the first azide-inhibited structure of this family of enzymes. The enzyme binds exogenous ligands such as cyanide and azide, which also inhibit the catalytic activity by coordinating the P heme iron, the active site, and competing with its substrate, hydrogen peroxide. The inhibition constants were estimated to be 0.4 ± 0.1 µM and 41 ± 5 mM for cyanide and azide, respectively. Imidazole also binds and inhibits the enzyme in a more complex mechanism by binding to P and E hemes, which changes the reduction potential of the latest heme. Based on the structures now reported, the catalytic cycle of bacterial peroxidases is revisited. The inhibition studies and the crystal structure of the inhibited enzyme comprise the first platform to search and develop inhibitors that target this enzyme as a possible new strategy against N. gonorrhoeae.

The cellulosome is an elaborate multi-enzyme structure secreted by many anaerobic microorganisms for the efficient degradation of lignocellulosic substrates. It is composed of multiple catalytic and non-catalytic components that are assembled through high-affinity protein-protein interactions between the enzyme-borne dockerin (Doc) modules and the repeated cohesin (Coh) modules present in primary scaffoldins. In some cellulosomes, primary scaffoldins can interact with adaptor and cell-anchoring scaffoldins to create structures of increasing complexity. The cellulosomal system of the ruminal bacterium, Ruminococcus flavefaciens, is one of the most intricate described to date. An unprecedent number of different Doc specificities results in an elaborate architecture, assembled exclusively through single-binding-mode type-III Coh-Doc interactions. However, a set of type-III Docs exhibits certain features associated with the classic dual-binding mode Coh-Doc interaction. Here, the structure of the adaptor scaffoldin-borne ScaH Doc in complex with the Coh from anchoring scaffoldin ScaE is described. This complex, unlike previously described type-III interactions in R. flavefaciens, was found to interact in a dual-binding mode. The key residues determining Coh recognition were also identified. This information was used to perform structure-informed protein engineering to change the electrostatic profile of the binding surface and to improve the affinity between the two modules. The results show that the nature of the residues in the ligand-binding surface plays a major role in Coh recognition and that Coh-Doc affinity can be manipulated through rational design, a key feature for the creation of designer cellulosomes or other affinity-based technologies using tailored Coh-Doc interactions.