Answer:
C Region
Explanation:
C Region contains all the liquids as 0 °C is the freezing point of water (Crystals of water are formed leaving it no more in the liquid state) and 100 °C is the boiling point (The water boils leaving it no more in the liquid state).
Hence, All liquids are contained in the C region.
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Hope this helped!
<h3>~AH1807</h3>
The molarity of aqueous lithium bromide, LiBr solution is 0.2 M
We'll begin by calculating the number of mole of Pb(NO₃)₂ in the solution.
- Volume = 10 mL = 10 / 1000 = 0.01 L
- Molarity of Pb(NO₃)₂ = 0.250 M
- Mole of Pb(NO₃)₂ =?
Mole = Molarity x Volume
Mole of Pb(NO₃)₂ = 0.25 × 0.01
Mole of Pb(NO₃)₂ = 0.0025 mole
Next, we shall determine the mole of LiBr required to react with 0.0025 mole of Pb(NO₃)₂
Pb(NO₃)₂ + 2LiBr —> PbBr₂ + 2LiNO₃
From the balanced equation above,
1 mole of Pb(NO₃)₂ reacted with 2 mole of LiBr.
Therefore,
0.0025 mole of Pb(NO₃)₂ will react with = 2 × 0.0025 = 0.005 mole of LiBr
Finally, we shall determine the molarity of the LiBr solution
- Mole = 0.005 mole
- Volume = 25 mL = 25 / 1000 = 0.025 L
- Molarity of LiBr =?
Molarity = mole / Volume
Molarity of LiBr = 0.005 / 0.025
Molarity of LiBr = 0.2 M
Learn more about molarity: brainly.com/question/10103895
Answer:
Explanation:
Hello there!
In this case, for these problems about collecting a gas over water, we must keep in mind that once the gas has been collected, the total pressure of the system is given by the atmospheric pressure, in this case 1.01 atm. Next, since we also have water in the mixture, we can write the following equation:
Thus, by solving for the pressure of nitrogen and using consistent units, we obtain:
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.
