Answer:
Mass = 90.28 g
Explanation:
Given data:
Mass of Ca(OH)₂ = ?
Volume of solution= 1.5 L
Molarity of solution = 0.81 M
Solution:
First of all we will calculate number of moles.
Molarity = number of moles / volume in L
by putting values,
0.81 M = Number of moles / 1.5 L
Number of moles = 0.81 M × 1.5 L
Number of moles = 1.22 mol
Mass of Ca(OH)₂ in gram:
Mass = number of moles × molar mass
Mass = 1.22 mol × 74.09 g/mol
Mass = 90.28 g
Answer:
\frac{dh}{dt}_{h=2cm} =\frac{40}{9\pi}\frac{cm}{2}
Explanation:
Hello,
The suitable differential equation for this case is:

As we're looking for the change in height with respect to the time, we need a relationship to achieve such as:

Of course,
.
Now, since the volume of a cone is
and the ratio
or
, the volume becomes:

We proceed to its differentiation:

Then, we compute 

Finally, at h=2:

Best regards.
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.
Answer:
- <u>No, you cannot dissolve 4.6 moles of copper sulfate, CuSO₄, in 1750mL of water.</u>
Explanation:
This question is part of a Post-Lab exercise sheet.
Such sheet include the saturation concentrations for several salts.
The saturation concentration of Copper Sulfate, CuSO₄, indicated in the table is 1.380M.
That means that 1.380 moles of copper sulfate is the maximum amount that can be dissolved in one liter of solution.
Find the molar concentration for 4.6 moles of copper sulfate in 1,750 mL of water.
You need to assume that the volume of water (1750mL) is the volume of the solution. This is, that the 4.6 moles of copper sulfate have a negligible volume.
<u>1. Volume in liters:</u>
- V = 1,750 mL × 1 liter / 1,000 mL = 1.75 liter
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<u>2. Molar concentration, molarity, M:</u>
- M = number of moles of solute / volume of solution in liters
- M = 4.6 moles / 1.75 liter = 2.6 M
Since the solution is saturated at 1.380M, you cannot reach the 2.6M concentration, meaning that you cannot dissolve 4.6 moles of copper sulfate, CuSO₄ in 1750mL of water.