Holotoxin disassembly by protein disulfide isomerase is less efficient for Escherichia coli heat-labile enterotoxin than cholera toxin

Cholera toxin (CT) and Escherichia coli heat-labile enterotoxin (LT) are structurally similar AB5-type protein toxins. They move from the cell surface to the endoplasmic reticulum where the A1 catalytic subunit is separated from its holotoxin by protein disulfide isomerase (PDI), thus allowing the dissociated A1 subunit to enter the cytosol for a toxic effect. Despite similar mechanisms of toxicity, CT is more potent than LT. The difference has been attributed to a more stable domain assembly for CT as compared to LT, but this explanation has not been directly tested and is arguable as toxin disassembly is an indispensable step in the cellular action of these toxins. We show here that PDI disassembles CT more efficiently than LT, which provides a possible explanation for the greater potency of the former toxin. Furthermore, direct examination of CT and LT domain assemblies found no difference in toxin stability. Using novel analytic geometry approaches, we provide a detailed characterization of the positioning of the A subunit with respect to the B pentamer and demonstrate significant differences in the interdomain architecture of CT and LT. Protein docking analysis further suggests that these global structural differences result in distinct modes of PDI-toxin interactions. Our results highlight previously overlooked structural differences between CT and LT that provide a new model for the PDI-assisted disassembly and differential potency of these toxins.

ANALYZE THE EFFECT OF TIME DELAY ON THE STABILITY OF HYBRID ACTIVE POWER FILTER

Hybrid Active Power Filter (HAPF) has highly effective in improving the power quality of power system. In this paper, a stable analysis of HAPF considering the time delay was made. The mathematical model of HAPF with time delay has been established. Based on that, the stable domain of the HAPF parameters was determined based on the Routh’s stability standard. Simulation results based on Matlab software have shown that: time delay has a marked impact on the stability of the HAPF system. This research has practical significance in the design and control of HAPF in real system.

Modulational Instability of Ion-Acoustic Waves in Pair-Ion Plasma

The modulational instability (MI) of ion-acoustic waves (IAWs) is examined theoretically in a four-component plasma system containing inertialess electrons featuring a non-thermal, non-extensive distribution, iso-thermal positrons, and positively as well as negatively charged inertial ions. In this connection, a non-linear Schrödinger equation (NLSE), which dominates the conditions for MI associated with IAWs, is obtained by using the reductive perturbation method. The numerical analysis of the NLSE reveals that the increment in non-thermality leads to a more unstable state, whereas the enhancement in non-extensivity introduces a less unstable state. It also signifies the bright (dark) ion-acoustic (IA) envelope solitons mode in the unstable (stable) domain. The conditions for MI and its growth rate in the unstable regime of the IAWs are vigorously modified by the different plasma parameters (viz., non-thermal, non-extensive q-distributed electron, iso-thermal positron, the ion charge state, the mass of the ion and positron, non-thermal parameter α, the temperature of electron and positron, etc.). Our findings may supplement and add to prior research in non-thermal, non-extensive electrons and iso-thermal positrons that can co-exist with positive as well as negative inertial ions.

Holotoxin Disassembly by Protein Disulfide Isomerase Is Less Efficient for Escherichia Coli Heat-labile Enterotoxin Than Cholera Toxin

Cholera toxin (CT) and Escherichia coli heat-labile enterotoxin (LT) are structurally similar AB5-type protein toxins. They move from the cell surface to the endoplasmic reticulum where the A1 catalytic subunit is separated from its holotoxin by protein disulfide isomerase (PDI), thus allowing the dissociated A1 subunit to enter the cytosol for a toxic effect. Despite similar mechanisms of toxicity, CT is more potent than LT. The difference has been attributed to a more stable domain assembly for CT as compared to LT, but this explanation has not been directly tested and is arguable as toxin disassembly is an indispensable step in the cellular action of these toxins. We show here that PDI disassembles CT more efficiently than LT, which provides a possible explanation for the greater potency of the former toxin. Furthermore, direct examination of CT and LT domain assemblies found no difference in toxin stability. Using novel analytic geometry approaches, we provide a detailed characterization of the positioning of the A subunit with respect to the B5 pentamer and demonstrate significant differences in the interdomain architecture of CT and LT. Protein docking analysis further shows that these global structural differences result in distinct modes of PDI-toxin interactions. Our results highlight previously overlooked structural differences between CT and LT that provide a new molecular explanation for the PDI-assisted disassembly and differential potency of these toxins.

Modulational Instability of Ion-Acoustic Waves and Associated Envelope Solitons in a Multi-Component Plasma

A generalized plasma model with inertial warm ions, inertialess iso-thermal electrons, super-thermal electrons and positrons is considered to theoretically investigate the modulational instability (MI) of ion-acoustic waves (IAWs). A standard nonlinear Schrödinger equation is derived by applying the reductive perturbation method. It is observed that the stable domain of the IAWs decreases with ion temperature but increases with electron temperature. It is also found that the stable domain increases by increasing (decreasing) the electron (ion) number density. The present results will be useful in understanding the conditions for MI of IAWs which are relevant to both space and laboratory plasmas.

Dynamic Analysis and Degenerate Hopf Bifurcation-Based Feedback Control of a Conservative Chaotic System and Its Circuit Simulation

A novel conservative chaotic system with no equilibrium is investigated in this study. Various dynamics such as the conservativeness, coexistence, symmetry, and invariance are presented. Furthermore, a partial-state feedback control scheme is proposed, and the stable domain of control parameters is analyzed based on the degenerate Hopf bifurcation. In order to verify the numerical simulation analysis, an analog circuit is designed. The simulation results show that the output of the analog circuit system can reproduce the numerical simulation results and verify the correctness of the theoretical analysis.

Domain walls in 4d $$ \mathcal{N} $$ = 1 SYM

4d$$ \mathcal{N} $$ N = 1 super Yang-Mills (SYM) with simply connected gauge group G has h gapped vacua arising from the spontaneously broken discrete R-symmetry, where h is the dual Coxeter number of G. Therefore, the theory admits stable domain walls interpolating between any two vacua, but it is a nonperturbative problem to determine the low energy theory on the domain wall. We put forward an explicit answer to this question for all the domain walls for G = SU(N), Sp(N), Spin(N) and G2, and for the minimal domain wall connecting neighboring vacua for arbitrary G. We propose that the domain wall theories support specific nontrivial topological quantum field theories (TQFTs), which include the Chern-Simons theory proposed long ago by Acharya-Vafa for SU(N). We provide nontrivial evidence for our proposals by exactly matching renormalization group invariant partition functions twisted by global symmetries of SYM computed in the ultraviolet with those computed in our proposed infrared TQFTs. A crucial element in this matching is constructing the Hilbert space of spin TQFTs, that is, theories that depend on the spin structure of spacetime and admit fermionic states — a subject we delve into in some detail.