Answer:
plant cell
Explanation:
The Golgi apparatus is a cell organelle responsible for modifying, sorting and packaging proteins and lipid molecules into vesicles (i.e., Golgi vesicles) for their delivery to targeted cell sites. A plant cell can contain many -even hundreds- of Golgi apparatus. During cell division of plant cells, Golgi vesicles combine at the metaphase plate in order to form a structure called phragmoplast. Subsequently, the cell plate formed by phragmoplast vesicles grows from the center to the cell walls. Finally, the vesicle membranes fuse to form a plasma membrane that divides the plant cell into two cells.
Answer:
false
Explanation:
These different faces are called phases and they are the result of the way the Sun lights the Moon's surface as the Moon orbits Earth. The Moon can only be seen as a result of the Sun's light reflecting off it. It does not produce any light of its own.
Answer:
the correct answer is DNA
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.
