Answer:
The resulting molarity is 6M.
Explanation:
A dilution consists of the decrease of concentration of a substance in a solution (the higher the volume of the solvent, the lower the concentration).
We use the formula for dilutions:
C1 x V1 = C2 x V2
12 M x 0,5L = C2 x 1,0 L
C2= (12 M x 0,5 L)/1,0 L
<em>C2= 6 M</em>
Answer:
Explanation:
Kinetic Molecular Theory states that gas particles are in constant motion and exhibit perfectly elastic collisions.The average kinetic energy of a collection of gas particles is directly proportional to absolute temperature only.
Answer:
atomic mass of X is 48.0 amu
Explanation:
Let y be the atomic mass of X
Molar mass of O_2 is = 2×16 = 32 g / mol
X + O2 -----> XO_2
According to the equation ,
y g of X reacts with 32 g of O_2
24 g of X reacts with Z g of O_2
Z = ( 32×24) / y
But given that 24.0 g of X exactly reacts with 16.0 g of O_2
So Z = 16.0
⇒ (32×24) / y = 16.0
⇒ y = (32×24) / 16
y= 48.0
So atomic mass of X is 48.0 amu
Answer:
c. By itself, heme is not a good oxygen carrier. It must be part of a larger protein to prevent oxidation of the iron.
e. Both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a central iron ( Fe ) (Fe) atom.
f. Hemoglobin is a heterotetramer, whereas myoglobin is a monomer. The heme prosthetic group is entirely buried within myoglobin.
Explanation:
The differences between hemoglobin and myoglobin are most important at the level of quaternary structure. Hemoglobin is a tetramer composed of two each of two types of closely related subunits, alpha and beta. Myoglobin is a monomer (so it doesn't have a quaternary structure at all). Myoglobin binds oxygen more tightly than does hemoglobin. This difference in binding energy reflects the movement of oxygen from the bloodstream to the cells, from hemoglobin to myoglobin.
Myoglobin binds oxygen
The binding of O 2 to myoglobin is a simple equilibrium reaction:
