Answer:
Explanation:
Less broadly, atheism is a rejection of the belief that any deities exist. In an even narrower sense, atheism is specifically the position that there are no deities. Atheism is contrasted with theism, which in its most general form is the belief that at least one deity exists.
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Answer:
This signifies that the protein primarily comprises multiple polypeptide chains connected together with the help of disulfide bonds. The enzymes may be found in the form of dimers, trimers, or tetramers. Various examples of dimers, trimers, and tetramer proteins are known, of them, NEMOs dimers are considered to be held by disulfide bonds.
Thus, it can be hypothesized that the enzyme under examination is a multimer held in combination by disulfide bonds, with each comprising catalytic sites. On breaking of disulfide bonds, the enzyme dissociates into its many single units.
This illustrates the reduction in catalytic activity. Each active site in a single unit will work, however, at a gradual rate. This also shows detection of multiple globular proteins after disulfide reduction.
These are the answers for questions 1-7 I wasn’t sure in 8 though
<span>Lafora disease is the most severe teenage-onset progressive epilepsy, a unique form of glycogenosis with perikaryal accumulation of an abnormal form of glycogen, and a neurodegenerative disorder exhibiting an unusual generalized organellar disintegration. The disease is caused by mutations of the EPM2A gene, which encodes two isoforms of the laforin protein tyrosine phosphatase, having alternate carboxyl termini, one localized in the cytoplasm (endoplasmic reticulum) and the other in the nucleus. To date, all documented disease mutations, including the knockout mouse model deletion, have been in the segment of the protein common to both isoforms. It is therefore not known whether dysfunction of the cytoplasmic, nuclear, or both isoforms leads to the disease. In the present work, we identify six novel mutations, one of which, c.950insT (Q319fs), is the first mutation specific to the cytoplasmic laforin isoform, implicating this isoform in disease pathogenesis. To confirm this mutation's deleterious effect on laforin, we studied the resultant protein's subcellular localization and function and show a drastic reduction in its phosphatase activity, despite maintenance of its location at the endoplasmic reticulum.
I got my information from </span>https://www.ncbi.nlm.nih.gov/pubmed/14722920
