Pressure Dependence of Structural and Mechanical Properties of Single-Crystal Tungsten: A Molecular Dynamics Study

In the current study, molecular dynamics (MD) simulations were performed to study the pressure dependence of the structural and mechanical properties of single-crystal tungsten. The results show that single-crystal tungsten possesses noteworthy high-pressure stability and exhibits linear lattice contraction with increasing external pressure. Consistent with the results of the performed experiments, the predicted elastic moduli, including Young’s modulus, shear modulus, and bulk modulus, as well as Poisson’s ratio and Pugh’s modulus ratio, show a clear increasing trend with the increase in pressure. Under uniaxial tensile loading, the single-crystal tungsten at high pressures experiences a phase transition from BCC to FCC and other disordered structures, which results in a stripe-like morphology in the tungsten crystal. These results are expected to deepen our understanding of the high-pressure structural and mechanical behaviors of tungsten materials.

Deciphering PD1 activation mechanism from molecular docking and molecular dynamic simulations

The activation of T cells is normally accompanied by inhibitory mechanisms within which the PD1 receptor stands out. Upon binding the ligands PDL1 and PDL2, PD1 drives T cells to an unresponsive state called exhaustion characterized by a markedly decreased capacity to exert effector functions. For this reason, PD1 has become one of the most important targets in cancer immunotherapy. Despite the numerous studies about PD1 signaling modulation, how the PD1 signaling is activated upon the ligands’ binding remains an open question. Several experimental facts suggest that the activation of the PD1-PLD1 pathway depends on the interaction with an unknown partner at the cellular membrane. In this work, we investigate the possibility that the target of PD1-PDL1 is the same PD1-PDL1 complex. We combined molecular docking to explore different binding modes with molecular dynamics and umbrella sampling simulations to assess the complexes’ stability. We found a high molecular weight complex that explains the activation of PD1 upon PDL1 binding. This complex has an affinity comparable to the PD1-PDL1 interaction and resembles the form of a linear lattice.

Macroscopic imprints of ductile deformation

The fundamentals of structural geology are presented, namely, folds, planar structures (cleavage or schistosity, foliation) and linear ones (lineations), regarded as emblematic for geologists. Ductile imprints of folds, affecting stratified formations, combined with brittle imprints, often remain modest in terms of strain intensity. Folding is essentially inhomogeneous and often results from the buckling (bending) of the layers (or stratification) as a consequence of layer parallel compression. Folded structures are frequently accompanied by fractures. Hence they may be classified as brittle–ductile. They are mostly encountered at low depths and constitute the upper structural level of the Earth’s crust. Ductile deformation sensu stricto appears at the lower structural level. The macroscopic aspects of ductile deformations and their implications will be examined. The principal operating mechanism, crystalline plasticity, represents the mechanical aspect of deformation, sometime assisted by chemical aspects (pressure-solution). While homogeneous deformation constitutes our principal concern, heterogeneous deformation is often present, particularly when examined at fine scales. At low shear strain (γ‎ < 0.7, or θ‎ ~35°, equivalent to ~30% shortening), plastic deformation generally leads to a planar and a linear anisotropy strengthening with increasing deformation. At higher shear strain, any pre-existing planar structure becomes so stretched that it cannot be recognized. The new structure may be purely planar, purely linear or plano-linear. Lattice fabrics, appearing in rocks subjected to plastic deformation and resulting from deformation mechanisms at the grain-scale, are examined in detail in Chapter 6.

On the ω-multiple Charlier polynomials

The main aim of this paper is to define and investigate more general multiple Charlier polynomials on the linear lattice $\omega \mathbb{N} = \{ 0,\omega ,2\omega ,\ldots \} $ ω N = { 0 , ω , 2 ω , … } , $\omega \in \mathbb{R}$ ω ∈ R . We call these polynomials ω-multiple Charlier polynomials. Some of their properties, such as the raising operator, the Rodrigues formula, an explicit representation and a generating function are obtained. Also an $( r+1 )$ ( r + 1 ) th order difference equation is given. As an example we consider the case $\omega =\frac{3}{2}$ ω = 3 2 and define $\frac{3}{2}$ 3 2 -multiple Charlier polynomials. It is also mentioned that, in the case $\omega =1$ ω = 1 , the obtained results coincide with the existing results of multiple Charlier polynomials.

Charge order textures induced by non-linear lattice coupling in a half-doped manganite

The self-organization of strongly interacting electrons into superlattice structures underlies the properties of many quantum materials. How these electrons arrange within the superlattice dictates what symmetries are broken and what ground states are stabilized. Here we show that cryogenic scanning transmission electron microscopy enables direct mapping of local symmetries and order at the intra-unit-cell level in the model charge-ordered system Nd1/2Sr1/2MnO3. In addition to imaging the prototypical site-centered charge order, we discover the nanoscale coexistence of an exotic intermediate state which mixes site and bond order and breaks inversion symmetry. We further show that nonlinear coupling of distinct lattice modes controls the selection between competing ground states. The results demonstrate the importance of lattice coupling for understanding and manipulating the character of electronic self-organization and highlight a novel method for probing local order in a broad range of strongly correlated systems.

Regulation of Actin Filament Length by Muscle Isoforms of Tropomyosin and Cofilin

In striated muscle the extent of the overlap between actin and myosin filaments contributes to the development of force. In slow twitch muscle fibers actin filaments are longer than in fast twitch fibers, but the mechanism which determines this difference is not well understood. We hypothesized that tropomyosin isoforms Tpm1.1 and Tpm3.12, the actin regulatory proteins, which are specific respectively for fast and slow muscle fibers, differently stabilize actin filaments and regulate severing of the filaments by cofilin-2. Using in vitro assays, we showed that Tpm3.12 bound to F-actin with almost 2-fold higher apparent binding constant (Kapp) than Tpm1.1. Cofilin2 reduced Kapp of both tropomyosin isoforms. In the presence of Tpm1.1 and Tpm3.12 the filaments were longer than unregulated F-actin by 25% and 40%, respectively. None of the tropomyosins affected the affinity of cofilin-2 for F-actin, but according to the linear lattice model both isoforms increased cofilin-2 binding to an isolated site and reduced binding cooperativity. The filaments decorated with Tpm1.1 and Tpm3.12 were severed by cofilin-2 more often than unregulated filaments, but depolymerization of the severed filaments was inhibited. The stabilization of the filaments by Tpm3.12 was more efficient, which can be attributed to lower dynamics of Tpm3.12 binding to actin.