From the med. terranian basin to the mountains of central asia.
He begins by discussing how horizontal transfer can move genetic material between bacteria. Transformation, transduction, and conjugation in bacteria are all included. He also explains how crossing over, random assortment, and random fertilization can maintain genetic variation in eukaryotes.
Answer:
It would be >> C plant cells
Answer:
1. A Struggle for Survival
2. survival will reproduce
3. Superior adaptive variation
Explanation:
1. Observation: overproduction of offspring that can possibly survive.
CONCLUSION: A Struggle for Survival, most of this offspring fight for food and water.
2. Observation: variation in species: member of the same species have different ways of identification, which are color, sex, e.t.c
CONCLUSION: Those individuals that survive and reproduce do so in consequence of "superior adaptive variation" (they are "more fit")
3. Observation: Variation heritable through selection: most survival pass there favourable adaptation to their offspring.
CONCLUSION: Superior adaptive variation will be passed on to offspring generation.
reference: https://www.mun.ca/biology/scarr/4250_History_II.html
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.
