Answer:
5: 0.16
6: 50
Explanation:
Question 5:
We can use the equation density = mass/ volume.
We already have the mass (12g), but now we need to find the volume of the cylinder.
The equation for this is πr²h
So we know the radius is 2 and the height is 6.
π x (2)² x 6 = 24π = 75.398cm³
Now we can use the density equation above:
12/75.398 = 0.1592g/cm³ = 0.16g/cm³.
Question 6:
This time, we have to rearrange the equation density = mass/ volume to find the mass.
We know mass = density x volume.
From the question, the density is 2.5g/mL and the volume is 20mL.
Following the equation above, we do 2.5 x 20 to get 50g.
... indicates that it also has a high concentration of Hydroxide (OH) and that it is more basic.
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:
false
true
true
Explanation:
false - changing the hypothesis to meet your needs is not a good researcher
true - when you can further analyze and explain then you have a successful experiment even if it's not what you expected
true - successful experiments do not end there. they can lead to more in depth questions.
