<span>BaCl2+Na2SO4---->BaSO4+2NaCl
There is 1.0g of BaCl2 and 1.0g of Na2SO4, which is the limiting reagent?
"First convert grams into moles"
1.0g BaCl2 * (1 mol BaCl2 / 208.2g BaCl2) = 4.8 x 10^-3 mol BaCl2
1.0g Na2SO4 * (1 mol Na2SO4 / 142.04g Na2SO4) = 7.0 x 10^-3 mol Na2SO4
(7.0 x 10^-3 mol Na2SO4 / 4.8 x 10^-3 mol BaCl2 ) = 1.5 mol Na2SO4 / mol BaCl2
"From this ratio compare it to the equation, BaCl2+Na2SO4---->BaSO4+2NaCl"
The equation shows that for every mol of BaCl2 requires 1 mol of Na2SO4. But we found that there is 1.5 mol of Na2SO4 per mol of BaCl2. Therefore, BaCl2 is the limiting reagent.</span>
Answer: P: 25.898% CI: 74.102 %
Explanation: Use the formula, Mass % = mass/total Mass x 100%, to solve.
<span>1.
London forces. 4. dipole - dipole. Due to a small hydrogen atom and a
much large fluorine atom, with a large , positive nuclus and large,
negative, p orbitals . This makes it very polar.</span>
Answer:
For these types of questions the equation that we must take into account is that:
T = PxV (where T is the temperature, P is the pressure and V is the volume) this equation is described as we consider that this is the value N and R is 1, therefore it is not necessary to explain them now.
Explanation:
The quoted equation refers to Boyle's Law, in this law we can explain that the volume increases if the pressure decreases and if the temperature also increases, if the pressure increases and the volume decreases this means that the gas is compressing assuming that the temperature is constant
Answer:
The protein has 4 subunits: 2 subunits of 90 kDa, 1 subunit of 160 kDa and 1 subunit of 60 kDa
Explanation:
In gel electrophoresis, the SDS agent produces denaturation of the protein and confers negative charge, so the protein subunits can migrate according to their masses. It produces dissociation of the protein in its subunits but it cannot disrupt disulphyde bridges (S-S) that can bond subunits together.
From the data, with SDS we observe 3 bands ⇒ 180 kDa + 160 kDa + 60 kDa
The addition of dithiotreitol (DTT), a reducing agent, produces the disruption of disulphyde bridges. From the data:
With DTT ⇒ 160 kDa + 90 kDa + 60 kDa
We observe that 160 kDa and 60 kDa subunits are conserved (they are the same as with SDS only), but 180 kDa subunit is missing and in its place appears a band of 90 kDa - a half 180 kDa.
So, the band at 180 kDa is composed by two subunits bonded by a disulphyde bridge.
Therefore, the composition of the protein is: <em>1 subunit of 160 kDa, 2 subunits of 90 kDa and 1 subunit of 60 kDa</em>.