Answer:soil that is a mixture of silt and clay
Explanation:
I got a 100%
Answer: A. Digest fats in the stomach.
Explanation: The liver produces bile. Bile emulsifies fats, It breaks up large droplets of fats into smaller droplets, thereby increasing the surface area for lipases to work on, speeding up the digestion of fat by the lipase. Bile further neutralizes the acid produced by the stomach to provide an alkaline environment for enzymes in the small intestine.
Bile acids are important for digestion and absorption of fats and fat-soluble vitamins in the small intestine.
Answer: Crossing over
Explanation:
In meiosis, chromatids are made to exchange their genetic material during Prophase to allow the formation of offspring that are genetically different from their parents.
The process of exchange is called CROSSING OVER. And it occurs through a contact point known as Chiasma.
Answer: to make sure that your getting all the right information for your needs
Explanation:
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.