Answer:
d. Measure thyroid-stimulating hormone level
Explanation:
The most suitable next step in management of this patient is to measure a thyroid stimulating hormone, or thyrotropin level.
This patient's apparent treatment refractory dyslipidemia is most likely contributed by undiagnosed thyroid disease. Despite sticking to the treatment with atorvastatin, his LDL AND total cholesterol are raised.
Additionally, there are some clinical signals that give an idea about the diagnosis of hypothyroidism especially fatigue and constipation.
Hypothyroidism is concerned with and is a very common secondary cause of dyslipidemia and thyrotropin level measures are indicated.
Hyperlipidemia may show better results to thyroid stimulating hormone.
Hence option D is the right answer.
Regarding human traits, Locke would most likely agree with Aristotle.
There are more areas where Aristotle and Locke's philosophical views diverge than where they concur. For instance, Aristotle once claimed that a person's happiness was just as important to them as it was to their political community. The political understanding of Locke, however, is different because, in his view, a government only assumes responsibility for a portion of the human rights that it is meant to protect in accordance with what people deem to be right. Individuals are therefore given priority because they have rights that are inalienable and shouldn't be manipulated by people to fit their agenda. These and other traditional philosophies have been used to analyze and comprehend early philosophy.
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Answer:
D. A mutualism relationship, because the fungus and algae both benefit from the relationship
Explanation:
The reason it's D is because a mutualism relationship means that both organisisms benefit from the relationship. Explained in the question, the fungus obtains the resources that the algae uses to make them both food.
Answer:
The options A, B, and D are all valid.
Explanation:
- The reason is that some proteins require molecular chaperones if they are to fold properly within the environment of the cell. In the absence of chaperones, a partially folded polypeptide chain has exposed amino acids that can form non-covalent bonds with other regions of the protein itself and with other proteins, thus causing nonspecific aggregation of proteins.
- The option A) is correct because the protein you are expressing in bacteria is being made in large quantities, it is possible that there are not enough chaperone molecules in the bacterium to fold the protein. Expressing the protein at lower levels might increase the amount of properly folded protein.
- The option B) is correct as urea should solubilize the protein and completely unfold it. Removing the urea slowly and gradually often allows the protein to refold. Presumably, under less crowded conditions, the protein should be able to refold into its proper conformation.
- The option C) is not correct as treating the aggregate with a protease, which cleaves peptide bonds, will probably solubilize the protein by trimming it into pieces that do not interact as strongly with one another; however, chopping up the protein will also destroy its enzymatic activity.
- The option D) is correct because overexpressing chaperone proteins might increase the amount of properly folded protein.
- The option E) is not correct as heating can lead to the partial denaturation and aggregation of proteins to form a solid gelatinous mass, as when cooking an egg white, and rarely helps solubilize proteins.
