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Throughout history, the United States invoked the Roosevelt Corollary to the Monroe Doctrine to accomplish some imperialistic and interventionists goals in different Central American and South American countries.
We can set some examples here. For instance, that was the case of the US intervention in the Island of Cuba, in Nicaragua, Dominican Republic, Hati, and the US presence for so many years in the Panama Canal.
Let's have in mind that the Roosevelt Corollary to the Monroe Doctrine was originally called for intervening in Latin American countries that could not pay their debt to European creditors.
The message the US wanted to convey to European superpowers that had interests in this region was that from now on, it was going to be the US business to intervene in the Americas. If Europe tried to intervene, it was going to be understood as direct aggression to the United States.
Answer: as the predator’s population goes up, the preys will go down, and as the prey’s goes up, the predators will go up. They are basically the opposite of each other.
Explanation: I can’t really tell what your question is. However if there are more prey to eat, then the number of predators will grow because they have more food. However, once there’s too many predators, the number of prey will drop which lowers the amount of food.
The chemical reactions in the cell would not happen as fast and would require more energy to catalyze the reaction between the two reactants.
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Chemistry/ Example: Take breathing for example, when you breath you breath out carbon dioxide. The CO2 can't just leave like that and only 10% binds to hemoglobin. The rest turns into carbonic acid in your blood and its plasma. However, the acid is unstable, so it turns into bicarbonate and a dissociated proton (H). You have carbonic anhydrase that converts the two so you can breath out CO2; the carbonic acid separates into H2O and CO2. This process would take a LONG time without the enzyme-- CO2 build up, even minimal amounts it lethal.
Answer:
as a dimer consisting of two identical monomers (80 kDa subunits) that are packed together via hydrophobic interactions
Explanation:
SDS-PAGE (sodium dodecyl sulphate–polyacrylamide gel electrophoresis), is an electrophoretic methodology used to separate proteins that have a molecular weight between 5 to 250 kDa. SDS is a well-known ionic detergent that is able to break hydrophobic interactions and hydrogen bonds. Moreover, size-exclusion chromatography is a filtration technique that separates molecules in solution according to their molecular size. In this case, SDS-PAGE showed that the target protein is composed of two identical subunits (monomers) of 80 kDa each, which were separated by the detergent and formed one single band in the SDS-PAGE gel.
