Answer:
Explanation:
The spores of some fungi are dispersed in water or on the surface of water. The chemical composition of the wall of these spores makes them "non-wettable" so they won't sink. The spores are carried along on the surface of the water like little boats. Water in the form of raindrops can disperse spores in a different way. While gravity is not a primary means of spore dispersal, evolutionary adaptations have been required of many fungi to overcome gravitational effects for effective spore dispersal. SPORE DISPERSAL BY WIND Dispersal of fungal spores by wind is by far the most common method for terrestrial fungi.
Answer: A. GTATTCGTGAATCCG
B: GGTCTCATCGGTCCA
Explanation:
G goes with C and A goes with T
Remember with a song:
Apples go in trees, Cars in the garage
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.
