I remember back in 10th grade I learned that birds that had beaks that were easier to break the seeds carried those traits to their babies and the whole area had that type of beak since it was necessary to break some seeds. So the beaks that were a disadvantage no longer existed and the beaks that became an advantage passed along to all the other birds.
Side note: if they all had the same beak they could all fight for the same type of seeds and probably have some sort of intense competition but idk if that’s necessary
Explanation:
Primordial organisms did not require oxygen for respiration as is the case with most organisms case today. These organisms were and are still mainly anaerobic. They main form of cellular respiration is glycolysis that does not utilize oxygen. Since other organisms evolved from the primordial cells, it is deduced that the early atmosphere was not mainly composed of oxygen but mainly carbon dioxide.
In today’s aerobic cells oxygen is utilized in the Krebs cycle as a proton acceptor making cellular respiration even more efficient in the production of energy. Remember that, utlimately, organisms evolve to fit into their environment.
Learn More:
For more on the early earth's atmosphere check out;
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Drinking through a straw shows fluid flowing from high pressure to low pressure in 2 ways. The first is how it shows high pressure as you stuck on the straw. This increases the pressure and brings the fluid to your mouth. If this pressure is kept you can successfully pick up the straw filled with water and have none come out. This demonstrates low pressure when you stop ducking and the fluid falls back down the straw into your cup.
<span>The correct answer is d. Antarctica must have been in a different warmer location in the past. The presence of Glossopteris in Antarctia proves that the continent was located closer to the equator and have since drifted to the south pole. This observation supports the theory of continental drift. </span>
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.
