Answer:
3 mol Cl₂/2 mol AlCl₃ (three over two)
Step-by-step explanation:
Start with the balanced equation"
2Al + 3Cl₂⟶ 2AlCl₃
The steps in the calculation are
mass of AlCl₃ ⟶ moles of AlCl₃⟶ moles of Cl₂ ⟶ mass of Cl₂
The critical step is the <em>conversion of moles</em>.
You multiply the moles of AlCl₃ by a <em>conversion factor</em> to get moles of Al:
Moles of AlCl₃ × conversion factor = moles of Al.
The conversion factor is <em>the molar ratio</em>, and it uses the coefficients of the formulas in the balanced equation.
It is either (2 mol AlCl₃/3 mol Cl₂) or (3 mol Cl₂/2 mol AlCl₃).
You choose the one that has the desired units of the answer in the numerator.
We choose the second option, because it has the correct units.
For example,
Notice how the units "mol AlCl₃" cancel and the correct units appear in the answer.
If we had used the other conversion factor, we would have gotten the wrong units.
Meanders, water<span> flows fastest on the outer bend of the river where the channel is deeper and there is less friction.</span>
First look at the molar mass of Al, which is 26.98 grams. That means that there are 26.98 grams in one mole of Al. To find the moles in your given sample of 64.1 grams, just divide that value by the molar mass of 26.98 grams. That will give you a final answer of 2.38 moles in 64.1 grams of Al.
Hope this helps!
Answer:
A. the rate of the acylation reaction being faster than the deacylation reaction.
Explanation:
Chymotrypsin belongs to a class of enzymes known as proteases; enzymes that catalyse the cleavage of peptide bonds by hydrolysis.
The mechanism of chymotrypsin catalysis occurs in two distinct phases; (1) an acylation phase where the peptide bond is cleaved and an ester linkage is formed between the peptide carbonyl carbon and the enzyme, (2) a deacylation phase where the ester linkage is hydrolyzed and the non-avylated enzyme is regenerated.
In studies by B.S. Hartley and B.A. Kilby in 1954 of chymotrypsin hydrolysis of the ester p-nitropheylacetate, as measured by the release of nitrophenol, it was discovered that it proceeded with a burst before leveling of to a slower rate. This burst was due to a rapid acylation of all the enzyme molecules with a slow deacylation limiting the turnover of the enzyme.
Similarly, the observation of burst kinetics in rapid kinetic studies of the hydrolysis of p-nitrophenylphosphate by chymotrypsin is due to the initial phase of acylation proceeding much faster than the later phase of deacylation of the enzyme.