Answer:
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12 grams
The mass of one mole of carbon-12 atoms is 12 grams.
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Explanation:
Answer:
Option 3. The catalyst does not affect the enthalpy change (
) of a reaction.
Explanation:
As its name suggests, the enthalpy change of a reaction () is the difference between the enthalpy of the products and the reactants.
On the other hand, a catalyst speeds up a reaction because it provides an alternative reaction pathway from the reactants to the products.
In effect, a catalyst reduces the activation energy of the reaction in both directions. The reactants and products of the reaction won't change. As a result, the difference in their enthalpies won't change, either. That's the same as saying that the enthalpy change of the reaction would stay the same.
Refer to an energy profile diagram. Enthalpy change of the reaction measures the difference between the two horizontal sections. Indeed, the catalyst lowered the height of the peak. However, that did not change the height of each horizontal section or the difference between them. Hence, the enthalpy change of the reaction stayed the same.
The answer is C. Arrhenius bases increase the concentration of OH- in solution.
The percentage composition of CF4 is %C = 13.64% and %F = 86.36%
The solution are as follows:
Molar mass of CF4 = 88
<span>molar mass of C = 12 </span>
<span>molar mass of F = 4x19 = 76 </span>
<span>% C = 12/88 x 100 = 13.64% </span>
<span>% F = 76/88 x 100 = 86.36%</span>
Answer:
The correct answer is: Serine, Histidine, Aspartate
Explanation:
The catalytic triad of an enzyme is composed of three aminoacid residues which are the most important for its catalytic activity. They are located in the catalytic site of the enzyme. In the case of chymotrypsin- a serine protease, the catalytic triad is composed by serine, histidine and aspartate (Ser-His-Asp). Serine proteases hydrolyse peptidic bonds in proteins and peptides. To do that, the histidine-which interacts with the aspartate by a hydrogen bond so its pKa increases- take a proton from the serine. Thus, deprotonated serine is able to attack the peptide bond and to perform hydrolysis.
