You should post the diagrams but basically there are more cells than tissues and more tissues than organs
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.
Answer:
a mutation that blocks the GTPase activity of Ras
Explanation:
A G protein in inactive state is GDP bound but as soon as a guanine exchange factor (GEF) exchanges it with GTP it gets activated which means that in GTP bound state it is active. G - protein has endogenous GTPase activity. Upon interaction of GAP, the GTPase activity of this protein is exhibited. When GAP is present, hydrolysis of GTP into GDP occurs which leads to inactivation of G protein. A mutation which will block GTPase activity of Ras will therefore result in constitutive active signaling even in the absence of ligand binding to it's receptor. In such scenario, GTP will not be hydrolyzed into GDP so signaling will be up-regulated.
Heredity/Hereditary
<span>(the passing on of physical or mental characteristics genetically from one generation to another) Physical features mainly. </span>
Carbon dioxide (CO2) is formed from one carbon atom bonded to two oxygen atoms. Therefore, carbon dioxide is a compound!
