Answer:
D) The equilibrium lies far to the left
Explanation:
According to the law of mass action, the equilibrium constant K for the reaction at 373K can be calculated as follows:
K = ![\frac{[CO][Cl_{2}]}{[COCl_{2}]}](https://tex.z-dn.net/?f=%5Cfrac%7B%5BCO%5D%5BCl_%7B2%7D%5D%7D%7B%5BCOCl_%7B2%7D%5D%7D)
= 2.19×10^{-10}
([X] means = concentration of X)
This means that in the equilibrium the concentration of the reactant (that is in the denominator) will be much higher (around 10^{10} fold) than the concentrations of the products (that are in the numerator), and this means that the equilibrium lies far to the left (to the reactants side) as very small amount of product is being formed.
Answer:
Explanation:
3.
Knowns: 100mL of solution; concentration of 0.7M
Unknown: number of moles
Equation: number of moles = volume * concentration
Plug and Chug: number of moles = 100/1000 * 0.7 = 0.07 mole
Final Answer: 0.07mole
2.
Knowns: 5.50L of solution; concentration of 0.400M
Unknown: number of moles
Equation: number of moles = volume * concentration
Plug and Chug: number of moles = 5.5 * 0.4 = 2.20 mole
Final Answer: 2.20 mole
If one were to match the ratio of atoms of the elements found in this molecular formula of artificial sweetener it would be :
Carbon - 7 atoms
Hydrogen - 5 atoms
Nitrogen - 1 atom
Oxygen - 3 atoms.
Physical. When you simply desolve something with water, to don't actually change it. This action can be undone.
An example of a chemical reaction is when the cells within completely change. You you burn wood, you can't go back in time and un-burn it. Does that make sense?
Answer:
The answer is IONIC BOND
Explanation:
Steroidogenic acute regulatory, (StAR) protein is a type of globular protein, which allows it act as an active catalyst on substrates. Because the substrates on which enzymes act usually have higher molecular weights of several hundred as compared to the enzymes, only a fraction of the enzyme's surface is in contact with the substrate. This region of contact called the <em>active site</em>, is as a result of the protein folding itself into a tertiary structure.
Once the correct substrate has bound at the active site of the enzyme, an enzyme-substrate complex is created. The substrate is usually held in the complex by combinations of electrical attraction, hydrophobic repulsion, or hydrogen bonding between and from the amino acid; the strongest of which is the ionic/electrostatic bonding due to larger amount of ionic "R" groups in the protein structure.
So whilst all these inter-molecular interactions are possible, the strongest would be <u>ionic bond.</u>
