This makes sense since most amino acids have no charge at all or very little charge. The less stable something is, the more energy it will use. The hydrophobic amino acids often are folded into the middle of the final protein structure to avoid instability. Chaperone cells are meant to assist with protein folding to make sure the protein folds into their correct shape. However, sometimes the up regulation or down regulation of these cells can cause the structure to not be folder properly. I'd expect to see more hydrophobic amino acids exposed when there's down regulation of chaperone cells. Is there an enzyme or drug that can be used to help control the regulation? From the reading, I took away that in the dominant-negative mechanism, the mutant protein is either dominant or co dominant to the wild type dominant protein. This causes the mutant protein to influence the function of the wild type dominant protein "negatively," or decreases its function. The mutant protein may completely take control over the dominant protein, or it may just decrease the dominant protein's activity. Proteins play a vital role in the way our bodies function and perform. After reading this article, it showed me how even a slight error or mutation can cause a lot of issues and cause diseases to form. Finding ways to help proteins conform to their proper shape can help cure many diseases. Understanding each level of protein structure is vital when finding cures to certain diseases and finding ways to manipulate protein shape to the correct conformation.
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