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3 years ago

Why does the solution decolorize on standing after the equivalence point has been reached?

Chemistry

2 answers:

Arisa [49]3 years ago

8 0

The equivalence point of a titration is equal to its stoichiometric equivalents of analyte and titrant.

Depending on the concentration of titrant we could be adding little excess of it and this may result in persistence of color of solution. After continuous stirring for a while the excess titrant may react with dissolved CO₂ in air and thus decolorizing the solution.

Colt1911 [192]3 years ago

3 0

Answer:

The potassium permanganate slowly fades in color as it is dissolved in the water.

Explanation:

Hello,

Perhaps, your talking about a titration that was carried out by using potassium permanganate as the titrant, thus, bringing to bear the fact that the equivalence point of a titration is equal to its stoichiometric equivalents of analyte and titrant, one could state that as the titration is carried out, the potassium permanganate slowly fades in color as it is dissolved in the water after the equivalence point is reached since the formed species become colorless as well.

Best regards.

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The Lewis structure of which molecule requires resonance structures?A.) MgCl2B.) SiO2C.) SO2D.) OCl2

inna [77]

Answer: C.) SO2

Explanation: Sulfur Dioxide is the gaseous molecule which can show the resonance through lewis dot structure due to the presence of lone pairs of electrons present on all of the three atoms of the molecules. Moreover , Sulphur forms pie bond with the oxygen using p orbitals which forms a network of the conjugated system that help to elaborate the reason of the formation of the resonance structure.

Options (a), (b), and (d) cannot form resonating structures as they involve the formation of the chemical bonds through single sigma bond.

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3 years ago

of an unknown protein are dissolved in enough solvent to make 5.00mL of solution. The osmotic pressure of this solution is measu

krok68 [10]

The question is incomplete . The complete question is :

100 mg of an unknown protein are dissolved in enough solvent to make 5.00mL of solution. The osmotic pressure of this solution is measured to be 0.107atm at 25.0°C. Calculate the molar mass of the protein. Round your answer to 3 significant digits.

Answer: The molar mass of the protein is $4.57\times 10^3g/mol$

Explanation:

$\pi =CRT$

$\pi=i\times \frac{\text{Mass of solute}\times 1000}{\text{Molar mass of solute}\times \text{Volume of solution (in mL)}}\times RT$

where,

$\pi$ = osmotic pressure of the solution = 0.107 atm

i = Van't hoff factor = 1 (for non-electrolytes)

Mass of solute (protein) = 100 mg = 0.1 g (Conversion factor: 1 g = 1000 mg)

Volume of solution = 5.00 mL

R = Gas constant = $0.0821\text{ L.atm }mol^{-1}K^{-1}$

T = temperature of the solution = $25^oC=[273+25]=298K$

Putting values in above equation, we get:

$0.107=1\times \frac{0.1\times 1000}{\text{Molar mass of insulin}\times 5.00}\times 0.0821\text{ Latm }mol^{-1}K^{-1}\times 298K\\\\\text{molar mass of protein}$

$\text{molar mass of protein}=4.57\times 10^3g/mol$

Hence, the molar mass of the protein is $4.57\times 10^3g/mol$

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2 years ago

When The appearance of a system changes does the mass of the system also change why why not

seropon [69]

No, because the appearance has nothing to do with system as well as the fact that appearance is only how it looks

(Btw, that toga picture is like... ughhhh!) hope this helps you ♥︎☀︎☁︎♨︎

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2 years ago

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Si agrega un ácido a una base, ¿qué pasará?

egoroff_w [7]

Answer:

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Explanation:

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3 years ago

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rjkz [21]

Answer:

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Explanation:

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