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Marriage is a primary and sacred need that is specifically regulated by religion. The sacred process in legalizing the relationship between men and women to prevent adultery and heinous acts. The multi-needs nature of marriage as a biological need and a social need must face problems with the Covid-19 virus that has hit all over the world and has stopped all social activities, including marriage. This article aims to examine how al-Ghazali with the construction of Maqāṣid al-Sharī'ah explores new laws in determining the permissibility of online marriage as a marriage solution during the Covid-19 pandemic. This research method uses a qualitative approach with the document study. The findings of this study: consideration of 4 (four) emergency arguments and “very ḍarar” dalil, and belongs to category categories of sensory ḍarar indrawi and ḍarar ‘ājilan. Assumptions offered by al-Ghazali include Al-Ḍarar Yazālu, Al-Ḍarar Yudfa'u Biqadri al-Imkāni considering the emergency conditions in which Al-Ḥājaṯ Tunzilu Manzilaṯ al-Ḍarūraṯ ‘Āmaṯ Kānata au Khāṣah and its Daf'a al-Qawāṭi'a. The conclusion of this study is that need for an online marriage that requires immediate action in the Covid-19 emergency because it is included in public and private problems around the world.

Marriage is a primary and sacred need that is specifically regulated by religion. The sacred process in legalizing the relationship between men and women to prevent adultery and heinous acts. The multi-needs nature of marriage as a biological need and a social need must face problems with the Covid-19 virus that has hit all over the world and has stopped all social activities, including marriage. This article aims to examine how al-Ghazali with the construction of Maqāṣid al-Sharī'ah explores new laws in determining the permissibility of online marriage as a marriage solution during the Covid-19 pandemic. This research method uses a qualitative approach with the document study. The findings of this study: consideration of 4 (four) emergency arguments and “very ḍarar” dalil, and belongs to category categories of sensory ḍarar indrawi and ḍarar ‘ājilan. Assumptions offered by al-Ghazali include Al-Ḍarar Yazālu, Al-Ḍarar Yudfa'u Biqadri al-Imkāni considering the emergency conditions in which Al-Ḥājaṯ Tunzilu Manzilaṯ al-Ḍarūraṯ ‘Āmaṯ Kānata au Khāṣah and its Daf'a al-Qawāṭi'a. The conclusion of this study is that need for an online marriage that requires immediate action in the Covid-19 emergency because it is included in public and private problems around the world.

Segmental duplications (SDs) or low-copy repeats, are segments of DNA > 1 Kbp with high sequence identity that are copied to other regions of the genome. SDs are among the most important sources of evolution, a common cause of genomic structural variation and several are associated with diseases of genomic origin including schizophrenia and autism. Despite their functional importance, SDs present one of the major hurdles for de novo genome assembly due to the ambiguity they cause in building and traversing both state-of-the-art overlap-layout-consensus and de Bruijn graphs. This causes SD regions to be misassembled, collapsed into a unique representation, or completely missing from assembled reference genomes for various organisms. In turn, this missing or incorrect information limits our ability to fully understand the evolution and the architecture of the genomes. Despite the essential need to accurately characterize SDs in assemblies, there has been only one tool that was developed for this purpose, called Whole-Genome Assembly Comparison (WGAC); its primary goal is SD detection. WGAC is comprised of several steps that employ different tools and custom scripts, which makes this strategy difficult and time consuming to use. Thus there is still a need for algorithms to characterize within-assembly SDs quickly, accurately, and in a user friendly manner., National Institutes of Health (U.S.) (Grant GM108348)

Segmental duplications (SDs), or low-copy repeats (LCR), are segments of DNA greater than 1 Kbp with high sequence identity that are copied to other regions of the genome. SDs are among the most important sources of evolution, a common cause of genomic structural variation, and several are associated with diseases of genomic origin. Despite their functional importance, SDs present one of the major hurdles for de novo genome assembly due to the ambiguity they cause in building and traversing both state-of-the-art overlap-layout-consensus and de Bruijn graphs. This causes SD regions to be misassembled, collapsed into a unique representation, or completely missing from assembled reference genomes for various organisms. In turn, this missing or incorrect information limits our ability to fully understand the evolution and the architecture of the genomes. Despite the essential need to accurately characterize SDs in assemblies, there is only one tool that has been developed for this purpose, called Whole Genome Assembly Comparison (WGAC). WGAC is comprised of several steps that employ different tools and custom scripts, which makes it difficult and time consuming to use. Thus there is still a need for algorithms to characterize within-assembly SDs quickly, accurately, and in a user friendly manner. Here we introduce a SEgmental Duplication Evaluation Framework (SEDEF) to rapidly detect SDs through sophisticated filtering strategies based on Jaccard similarity and local chaining. We show that SEDEF accurately detects SDs while maintaining substantial speed up over WGAC that translates into practical run times of minutes instead of weeks. Notably, our algorithm captures up to 25% pairwise error between segments, where previous studies focused on only 10%, allowing us to more deeply track the evolutionary history of the genome. SEDEF is available at https://github.com/vpc-ccg/sedef

Some properties of the K141E mutant of human HSP22 that is expressed in distal hereditary motor neuropathy were investigated. This mutation slightly decreased intrinsic fluorescence of HSP22 and induced changes in the far UV CD spectra that correlate with increase of disordered structure. Destabilized K141E mutant was more susceptible to trypsinolysis than the wild type protein. Mutation K141E did not significantly affect the hydrophobic properties measured by bis-ANS binding and did not affect the quaternary structure of HSP22. With insulin as a substrate the chaperone-like activity of K141E mutant and the wild type protein were similar. However with alcohol dehydrogenase and rhodanese the chaperone-like activity of K141E mutant was remarkably lower than the corresponding activity of the wild type protein. It is concluded that K141E mutation induces destabilization of HSP22 structure and probably by this means diminish the chaperone-like activity of HSP22 with certain protein substrates.

The recently described protein denoted H11, Hsp22 or HspB8 seems to participate in regulation of proliferation, apoptosis, and cardiac hypertrophy. Mutation of Hsp22 causes distal motor neuropathy. Multitude action of Hsp22 is supposed to be due to its protein kinase and/or chaperone-like activities. There are many indirect evidences indicating that Hsp22 possesses intrinsic protein kinase activity. However, low homology to protein kinases, low extent of autophosphorylation, lack of significant protein kinase activity with commonly used substrates, and lack of information on stoichiometry, kinetics, and substrate specificity make the existence of intrinsic protein kinase activity of Hsp22 questionable. It is supposed that protein kinase activity ascribed to Hsp22 is due to contaminating protein kinases. Hsp22 is highly homologous to small heat shock proteins and effectively prevents aggregation of denatured protein both in vitro and in vivo. Therefore, it is supposed that chaperone-like activity is of great importance for Hsp22 functioning.

Untagged recombinant human small heat shock protein with apparent molecular mass 22 kDa (Hsp22) was obtained in homogeneous state. Size exclusion chromatography and chemical crosslinking with dimethylsuberimidate indicate that Hsp22 forms stable dimers. Being highly susceptible to oxidation Hsp22 forms disulfide crosslinked dimers and poorly soluble high molecular mass oligomers. According to CD spectroscopy oxidation of Hsp22 results in disturbing of both secondary and tertiary structure. Hsp22 possesses a negligibly low autophosphorylation activity and under the conditions used is unable to phosphorylate casein or histone. Hsp22 effectively prevents heat-induced aggregation of yeast alcohol dehydrogenase and bovine liver rhodanese with chaperone activity comparable to that of recombinant human small heat shock protein with apparent molecular mass 20 kDa (Hsp20).