RESUMEN
The coupling of AC and DC power will impact the protective actions on the AC side and pose a threat to the stable operation of the interconnection system. Therefore, a new longitudinal protection method is proposed based on the comprehensive distance similarity of voltage waveforms. Initially, the measured voltage and current data are extracted to calculate the reference voltage, and the voltage waveform fitting is optimized. Subsequently, the Euclidean dynamic time warp (DTW) distance and entropy weight method are utilized to process the voltage waveform, enabling the calculation of its comprehensive distance similarity. This similarity is adopted to determine fault location. A hybrid DC multi-feed AC/DC interconnection system, incorporating a line commutated converter-voltage source converter (LCC-VSC) and a line commutated converter-modular multilevel converter (LCC-MMC), was established in PSCAD, and fault data were simulated and output. The effectiveness of the protection scheme was validated using MATLAB. Simulation results demonstrate that the proposed method can accurately distinguish between faults inside and outside a region. When compared to existing protection methods, it demonstrates superior performance in resisting transition resistance and noise interference, while also mitigating the impact of data asynchronicity. The speed and reliability of the method are further enhanced.
RESUMEN
Knowledge of the molecular mechanisms of specific bacterial virulence factors can significantly contribute to antibacterial drug discovery. Helicobacter pylori is a Gram-negative microaerophilic bacterium that infects almost half of the world's population, leading to gastric disorders and even gastric cancer. H. pylori expresses a series of virulence factors in the host, among which high-temperature requirement A (HpHtrA) is a newly identified serine protease secreted by H. pylori. HpHtrA cleaves the extracellular domain of the epithelial cell surface adhesion protein E-cadherin and disrupts gastric epithelial cell junctions, allowing H. pylori to access the intercellular space. Here we report the first crystal structure of HpHtrA at 3.0 Å resolution. The structure revealed a new type of HtrA protease trimer stabilized by unique N-terminal domain swapping distinct from other known HtrA homologs. We further observed that truncation of the N terminus completely abrogates HpHtrA trimer formation as well as protease activity. In the presence of unfolded substrate, HpHtrA assembled into cage-like 12-mers or 24-mers. Combining crystallographic, biochemical, and mutagenic data, we propose a mechanistic model of how HpHtrA recognizes and cleaves the well-folded E-cadherin substrate. Our study provides a fundamental basis for the development of anti-H. pylori agents by using a previously uncharacterized HtrA protease as a target.