The correct answer for the question is B, ATP contains less potential energy than ADP.
Explanation;
ATP contains more energy potential than ADP , since it has three phosphate bonds unlike ADP which has 2 phosphates.
A. is true; During glycolysis ATP is formed, Glycolysis uses 2 ATP molecules and also generates four ATP molecules which gives a net energy of 2 ATP molecules.
C is true, as plant cells generate ATP during cellular respiration. Cellular respiration is the process in which cells generate energy in form of ATP through oxidative phosphorylation in the mitochondria.
D. is true; ATP is used as a mobile energy carrier molecule by all cells. It used by these cells to fuel all cellular activities.
The air begins to rise into the atmosphere. When air rises, it cools down and condenses into precipitation and clouds. This is why an approaching low pressure system means an increased chance for clouds, rain, or snow. It is called "low pressure" because as air rises, the air pressure is lower at the surface.
Answer:
2x-2
Explanation:
2(x-3)+4
Distribute the 2 => 2x-6+4
Simplify => 2x-2
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.
False wes.j Moore was not close to his father
