A because the end result of this reaction is a radical created by the oxidation of an aromatic amine's or phenol's ring substituent. The hydroxyl group of a phenol acts as the ring substituent in this situation.
<h3>Which two enzyme types are required for the two-step process of converting cytosine to 5 hmC?</h3>
- The methyl group is transferred to cytosine in the first stage, and it is then hydroxylated in the second step.
- Therefore, a transferase and an oxidoreductase are the two groups of enzymes required.
<h3>Which kind of interaction between proteins and the dextran column material is most likely to take place?</h3>
- Hydrogen bonding because the glucose's OH would form an H-bond with any exposed polar side chains on a protein surface.
<h3>Two out of the four proteins would adhere to a cation-exchange column at what buffer pH? </h3>
- Only positively charged proteins can bind to a cation-exchange column, and this can only happen when the pH is lower than the pI.
- Proteins A and B would both be positively charged at pH 7.0.
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Answer:
2.
Explanation:
When you put the paper in a solution, it will turn blue if it is basic, or red if it is acidic. If it does not change color, it is fairly neutral.
Answer:
D. the organism is able to survive and reproduce more than others in it's environment
Explanation:
It will only go extinct if it can't survive or reproduce.
Answer:
C. The reaction is energetically favorable.
Explanation:
The reaction which shows the removal of the terminal phosphate from the ATP is shown below:

The Gibbs' free energy change of this reaction, 
Hence, Option A is not correct.
It is a type of hydrolysis reaction in which water is being added to the molecule.
Hence, Option B is not correct.
The Gibbs' free energy change is negative which means that the reaction is energetically favorable.
Option C is correct.
Answer:
Energy cannot be created or destroyed.
Explanation:
The Law of Conservation of Energy states that energy cannot be created nor destroyed, only converted from one form of energy to another.