代写论文-e -选择素配体的糖基化途径。众所周知，糖基化是糖分子与蛋白质的结合。有些蛋白质在这段时间内没有按照要求折叠以继续生化途径，糖基化是必需的。糖基化有两个作用。由于这种存在，它们具有一种直接的稳定性。在内质网内的糖蛋白折叠过程中，它们也是质量控制的表观遗传因子。除此之外，它们在细胞分子的粘附中起着重要的作用。由于这些，身体的许多过程依赖于糖基化过程。在这个过程中，身体里有特定的基因。本分析探讨了e -选择素配体的糖基化途径，并对其进行了详细的阐述。接下来代写论文-e -选择素配体的糖基化途径分享给留学生阅读。
It is a known fact that glycosylation is the attachment of the sugar molecules to the proteins. Some proteins do not fold according to the requirement to continue the biochemical pathways during those times, and glycosylation is required. Glycosylation serves two functions [35]. They have a direct stability occurring owing to this presence. They also serve as a quality control epigenetic factor in the glycoprotein folding within the Endoplasmic reticulum. Apart from this, they play an important role in the adhesion of cell molecules. Owing to these, a number of processes in the body are dependent on the glycosylation process. There are specific genes in the body that aids in this process.
During the cases of Cancer, there is aberrance observed in these actions. This leads to the cancer and tumor progression. There is a need to control this aberrant glycosylation. Hence, the glycosylation pathway in the case of E-selectin ligand has been probed in this analysis to elucidate it in detail. Fundamentally, those processes are explored in the following. There are two kinds of these glycosylation, they are the N-linked glycosylation and the O-lonked glycosylation [39]. In N-linked glycosylation, it has been found that the nitrogen atom binds to the ologisaccharide link. It has been found that Oligosaccharyltransferase (OST) plays a prominent role in the binding of the oligosachharide to the Nitrogen atom [40]. In reality, it has been found that this protein modification system is actually present in all life forms. It is based on the characterization of the species and is found differentiated by a large number of proteins that are glycosylated.
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