Answer:
A= 20%
G= 30%
T= 20%
C= 30%
Explanation:
Recall that the sum of all nitrogenous bases in the DNA nucleotide is equal to 100%. And specific base pairings of Adenine to Thymine (A=T), and Cytosine to Guanine (C=G) must be equal.
So, the percentage of Adenine equal thymine, and that of cytosine equals guanine.
Now, A + T + C + G = 100%
So, if Adenine makes up 20% of the DNA nucleotides, Thymine is also 20%.
Then, 20% + 20% + C + G = 100%
40% + C + G = 100%
C + G = 100% - 40% = 60%
So, divide 60% by 2 to obtain the individual percentage of cytosine and guanine. Each will take 30%
Finally, A= 20%; G= 30%; T= 20%; C= 30%
Answer:
Another important class of compounds produced by biotechnology is enzymes. One of the most significant commercial enzymes of this type is subtilisin, which is produced by a bacterium because many stains contain proteins, the manufacturers of laundry detergents include subtilisin in their product.
Explanation:
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A plant cell contains a large, singular vacuole that is used for storage and maintaining the shape of the cell. In contrast, animal cells have many, smaller vacuoles. Plant cells have a cell wall, as well as a cell membrane. ... Animal cells simply have a cell membrane, but no cell wall.
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.
