Answer: The most likely partial pressures are 98.7MPa for NO₂ and 101.3MPa for N₂O₄
Explanation: To determine the partial pressures of each gas after the increase of pressure, it can be used the equilibrium constant Kp.
For the reaction 2NO₂ ⇄ N₂O₄, the equilibrium constant is:
Kp = 
where:
P(N₂O₄) and P(NO₂) are the partial pressure of each gas.
Calculating constant:
Kp = 
Kp = 0.0104
After the weights, the total pressure increase to 200 MPa. However, at equilibrium, the constant is the same.
P(N₂O₄) + P(NO₂) = 200
P(N₂O₄) = 200 - P(NO₂)
Kp = 
0.0104 = ![\frac{200 - P(NO_{2}) }{[P(NO_{2} )]^{2}}](https://tex.z-dn.net/?f=%5Cfrac%7B200%20-%20P%28NO_%7B2%7D%29%20%20%7D%7B%5BP%28NO_%7B2%7D%20%29%5D%5E%7B2%7D%7D)
0.0104
+
- 200 = 0
Resolving the second degree equation:
=
= 98.7
Find partial pressure of N₂O₄:
P(N₂O₄) = 200 - P(NO₂)
P(N₂O₄) = 200 - 98.7
P(N₂O₄) = 101.3
The partial pressures are
= 98.7 MPa and P(N₂O₄) = 101.3 MPa
Answer:
an ice cube and paper cube with the same dimensions
Explanation:
an example is an ice cube and a cube with the same dimensions made of paper. these have the same volume, but different masses because the particles are packed differently and in different amounts.
Answer:
B and C
Explanation:
When we have to do a buffer solution we always have to choose the reaction that has the <u>pKa closer to the desired pH value</u>. When we find the pKa values we will obtain:
![pKa_1=-Log[6.9x10^-^3]=2.16](https://tex.z-dn.net/?f=pKa_1%3D-Log%5B6.9x10%5E-%5E3%5D%3D2.16)
![pKa_2=-Log[6.2x10^-^8]=7.20](https://tex.z-dn.net/?f=pKa_2%3D-Log%5B6.2x10%5E-%5E8%5D%3D7.20)
![pKa_3=-Log[4.8x10^-^13]=12.31](https://tex.z-dn.net/?f=pKa_3%3D-Log%5B4.8x10%5E-%5E13%5D%3D12.31)
The closer value is pKa2 with a value of 7.2. Therefore we have to use the second reaction. In which
is the <u>acid</u> and
is the <u>base</u>. Therefore the answer for the first question is B and the answer for the second question is C.
Answer:
A.
Explanation:
The <u>tertiary structure </u>of proteins is related to the interactions between the amino acids of the <u>primary structure</u>. Thus, these interactions give it a specific three-dimensional configuration which is very sensitive to <u>functionality</u>.
For example, <u>allosteric inhibitions</u> are related to this concept. When the <u>inhibitor</u> changes the tertiary structure of the protein it loses all <u>activity</u> and for the catalysis of the reaction.
Thus, the primary structure (which is related to the specific <u>sequence of amino acids</u>) will determine the tertiary structure since the chain folds will be a consequence of<u> intra-amino acid interactions</u>.