RESUMEN
Stroke patients under the background of the new crown epidemic need to be home-based care. However, traditional nursing methods cannot take care of the patients' lives in all aspects. Based on this, based on machine learning algorithms, our work combines regression models and SVM to build a smart wearable device system and builds a system prediction module to predict patient care needs. The node is used to collect human body motion and physiological parameter information and transmit data wirelessly. The software is used to quickly process and analyze the various motion and physiological parameters of the patient and save the analysis and processing structure in the database. By comparing the results of nursing intervention experiments, we can see that the smart wearable device designed in this paper has a certain effect in stroke care.
RESUMEN
[This corrects the article DOI: 10.1007/s00779-021-01520-9.].
Asunto(s)
COVID-19 , Humanos , COVID-19/epidemiología , Pandemias , SARS-CoV-2 , Cooperación InternacionalRESUMEN
The C-terminal domain of SARS-CoV main protease (Mpro-C) can form 3D domain-swapped dimer by exchanging the α1-helices fully buried inside the protein hydrophobic core, under non-denaturing conditions. Here, we report that Mpro-C can also form amyloid fibrils under the 3D domain-swappable conditions in vitro, and the fibrils are not formed through runaway/propagated domain swapping. It is found that there are positive correlations between the rates of domain swapping dimerization and amyloid fibrillation at different temperatures, and for different mutants. However, some Mpro-C mutants incapable of 3D domain swapping can still form amyloid fibrils, indicating that 3D domain swapping is not essential for amyloid fibrillation. Furthermore, NMR H/D exchange data and molecular dynamics simulation results suggest that the protofibril core region tends to unpack at the early stage of 3D domain swapping, so that the amyloid fibrillation can proceed during the 3D domain swapping process. We propose that 3D domain swapping makes it possible for the unpacking of the amyloidogenic fragment of the protein and thus accelerates the amyloid fibrillation process kinetically, which explains the well-documented correlations between amyloid fibrillation and 3D domain swapping observed in many proteins.