Answer:
They can preserve food in the cans, in the refrigerator and make them frozen, in the green houses to preserve them in the off season.
This is all how you can preserve food in the off season.
<h3>Hope this helps.</h3><h3>Good luck ✅.</h3>
The correct answer is: 5) NER recognizes helix distortions, while BER recognizes specific base damage.
DNA damage that occurs as a result of radiation, oxidizing reagents, chemicals and other mutagens can be repaired. Excision repair repairs single strand DNA damage and it includes:
• Nucleotide excision repair (NER)-it detects and repairs types of damage that distort the DNA double helix such as those of UV radiation (thymine dimers); not only the damaged nucleotide(s) are removed but also a surrounding patch of DNA
• Base excision repair (BER)-it detects and removes certain types of damaged bases (small, non-helix-distorting bases); enzyme glycosylase is responsible for this type of repair
Answer:
It should be letter D hope it helps
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.
Answer: the pioneer species
Explanation:
