The concentration of the sodium chloride would be 0.082 M
<h3>Stoichiometric calculations</h3>
From the equation of the reaction, the ratio of AgCl produced to NaCl required is 1:1.
Mole of 46.6 g AgCl produced = 46.6/143.32 = 0.325 moles
Equivalent mole of NaCl = 0.325 moles.
Molarity of 0.325 moles, 3.95 L NaCl = mole/volume = 0.325/3.95 = 0.082 M
More on stoichiometric calculations can be found here: brainly.com/question/27287858
#SPJ1
Answer:
310.53 g of Cu.
Explanation:
The balanced equation for the reaction is given below:
CuSO₄ + Zn —> ZnSO₄ + Cu
Next, we shall determine the mass of CuSO₄ that reacted and the mass Cu produced from the balanced equation. This can be obtained as follow:
Molar mass of CuSO₄ = 63.5 + 32 + (16×4)
= 63.5 + 32 + 64
= 159.5 g/mol
Mass of CuSO₄ from the balanced equation = 1 × 159.5 = 159.5 g
Molar mass of Cu = 63.5 g/mol
Mass of Cu from the balanced equation = 1 × 63.5 = 63.5 g
Summary:
From the balanced equation above,
159.5 g of CuSO₄ reacted to produce 63.5 g of Cu.
Finally, we shall determine the mass of Cu produced by the reaction of 780 g of CuSO₄. This can be obtained as follow:
From the balanced equation above,
159.5 g of CuSO₄ reacted to produce 63.5 g of Cu.
Therefore, 780 g of CuSO₄ will react to produce = (780 × 63.5)/159.5 = 310.53 g of Cu.
Thus, 310.53 g of Cu were obtained from the reaction.
The third reason helped Rutherford to discover the nucleus.
<h3><u>Answer;</u></h3>
The statements that are True are;
- Upon binding a molecule of oxygen, Hb undergoes a conformational change that makes the binding of subsequent O2 molecules easier.
- The conformational change induced in Hb upon binding oxygen is the result of a small movement (0.2 Å) of the iron cation in the center of heme.
- Site-directed mutagenesis studies have indicated that the cooperativity of O2 binding in Hb is attributable to the movement of the F helix in Hb.
<h3><u>Explanation</u>;</h3>
- Hemoglobin is a key pigment in the blood that transports oxygen gas to all the tissues in the body. It is made up of two types of chains; that is two alpha chains and two beta chains.
- in its deoxygenated state hemoglobin has a low affinity for oxygen compared to myoglobin. When oxygen is bound to the first subunit of hemoglobin it leads to subtle changes to the quaternary structure of the protein. This in turn makes it easier for a subsequent molecule of oxygen to bind to the next subunit.
