Answer:
33/7
Multiply the denominator of the fraction by the whole number.
Add this result to the numerator of the fraction
answer becomes the numerator of the improper fraction.
Explanation:
If in the solution, half of the added solute fails to dissolve. The solution started out supersaturated. The correct option is b.
<h3>What is supersaturation?</h3>
Supersaturation is the condition where the solutes exceed the amount that can be dissolved in a solution.
Supersaturation occurs when the solute no longer mix in the solution.
Thus, the correct option is b. The solution started out supersaturated.
Learn more about supersaturation
brainly.com/question/16817894
#SPJ1
Explanation:
When solid cadmium sulfide reacts with an aqueous solution of sulfuric acid then the reaction will be as follows.
Hence, ionic equation for this reaction is as follows.
Therefore, net ionic equation for this reaction is as follows.
Explanation:
To calculate the number of atoms in a sample, divide its weight in grams by the amu atomic mass from the periodic table, then multiply the result by Avogadro's number: 6.02 x 10^23.
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.
