Answer:
Volcanic degassing of volatiles, including water vapour, occurred during the early stages of crustal formation and gave rise to the atmosphere. When the surface of Earth had cooled to below 100 °C (212 °F), the hot water vapour in the atmosphere would have condensed to form the early oceans.
Explanation:
I think from the above answers the most appropriate is that GPS technology has led to development of robotic tractors for planting, fertilization, and crop harvesting. The global positioning system has found a wide and beneficial use in agriculture, it is used for mapping yields, variable rate planting, variable rate lime and fertilizer application, field mapping for records and insurance purposes among other uses.
A verified animal source such as animal planet or any website that doesn't have ads and has accurate info
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.
