Answer:
There are other details missing in the question. i.e Assume that x is much larger than the separation d between the charges in the dipole, so that the approximate expression for the electric field along the dipole axis E = p/2πε0y3 can be used, where p is the dipole moment, and y is the distance between ions. A) What is magnitude______N B) Direction? +x-direction or -x-direction C) Is this force attractive or repulsive?
A) Magnitude of electric force = 6.576 x 10 raised to power -13 N
B) Since the force direction is always dependent on the electric field and electric field = F/q, since the chlorine has a negative charge as such the direction of the electric force will be in the X - direction
C) Since the charges are of different nature, as such the force between them will be ATTRACTIVE.
Explanation:
The detailed steps is shown in the attachment
One is rows the other is columns
Answer:
2-Butanone
Explanation:
From the given information:
The presence of mercury as an acid catalyst brings about the addition of water to the triple bond which yields enol. Then, according to Markownikov's rule and after tautomerism has occurred, we have a methyl ketone ( 2- Butanone) as the product.
The answer regarding the transformation is addition and hydration.
Answer: Option (a) is the correct answer.
Explanation:
A protein part of an enzyme is known as an apoenzyme. An apoenzyme combines with a cofactor, it is known as holoenzyme.
Without a cofactor an apoenzyme cannot function as cofactor helps in the formation of an active enzyme system and provides a specific site on enzyme for the substrate.
Whereas a non-protein chemical compound or metal ion that helps in the activity of enzyme as a catalyst is known as a cofactor. A metal ion cofactor can be bound directly to the enzyme or to a coenzyme.
The organic non-protein molecules which bind to the protein molecule to form an active enzyme is known as a coenzyme. Coenzymes are small size molecules which help the enzymes to act as a catalyst.
Therefore, we can conclude that the statement an apoenzyme can catalyze its reaction without its cofactor, is false.