Answer:
May I assume "ethanol acid is just ethanol (it has one slightly acidic H atom). If so, the molar mass is 46.02 g/mole.
Explanation:
We have 30 cm^3 [30 ml] of 1.0 M (1 mole/liter) [1 dm³ = 1 liter].
That is 1 mole/liter. 30 ml would contain (0.030 liter)*(1 mole/1 liter) = 0.03 moles.
Answer:
A mixture of 100. mL of 0.1 M HC3H5O3 and 50. mL of NaOH
Explanation:
The pH of a buffer solution is calculated using following relation
Thus the pH of buffer solution will be near to the pKa of the acid used in making the buffer solution.
The pKa value of HC₃H₅O₃ acid is more closer to required pH = 4 than CH₃NH₃⁺ acid.
pKa = -log [Ka]
For HC₃H₅O₃
pKa = 3.1
For CH₃NH₃⁺
pKa = 10.64
pKb = 14-10.64 = 3.36 [Thus the pKb of this acid is also near to required pH value)
A mixture of 100. mL of 0.1 M HC3H5O3 and 50. mL of NaOH
Half of the acid will get neutralized by the given base and thus will result in equal concentration of both the weak acid and the salt making the pH just equal to the pKa value.
Answer:
The lock-and-key model:
c. Enzyme active site has a rigid structure complementary
The induced-fit model:
a. Enzyme conformation changes when it binds the substrate so the active site fits the substrate.
Common to both The lock-and-key model and The induced-fit model:
b. Substrate binds to the enzyme at the active site, forming an enzyme-substrate complex.
d. Substrate binds to the enzyme through non-covalent interactions
Explanation:
Generally, the catalytic power of enzymes are due to transient covalent bonds formed between an enzyme's catalytic functional group and a substrate as well as non-covalent interactions between substrate and enzyme which lowers the activation energy of the reaction. This applies to both the lock-and-key model as well as induced-fit mode of enzyme catalysis.
The lock and key model of enzyme catalysis and specificity proposes that enzymes are structurally complementary to their substrates such that they fit like a lock and key. This complementary nature of the enzyme and its substrates ensures that only a substrate that is complementary to the enzyme's active site can bind to it for catalysis to proceed. this is known as the specificity of an enzyme to a particular substrate.
The induced-fit mode proposes that binding of substrate to the active site of an enzyme induces conformational changes in the enzyme which better positions various functional groups on the enzyme into the proper position to catalyse the reaction.
We need an equation that will relate the concentrated mixture and the diluted one. To solve this we use the equation,
M1 V1 = M2 V2
where M1 is the concentration
of the stock solution, V1 is the volume of the stock solution, M2 is the
concentration of the new solution and V2 is its volume.
M1V1 = M2V2
30 % x 6 oz = 20 % x V2
V2 = 9 oz
The volume of the diluted mixture would be 9 oz. Therefore, you will need to add 9 oz - 6 oz = 3 oz of fruit juice to dilute the 30 percent alcohol to 20 percent alcohol.
