C. pouring honey on a plate so the density of thickness and stickyness would
be the highest
Answer is: line be long 3,011·10¹³ kilometers.
diametar of virus = 5·10⁻⁶ cm ÷ 100000 = 5·10⁻¹¹ km.
line lenght = 5·10⁻¹¹ km · 6,023·10²³.
line lenght = 3,011·10¹³ km.
Avogadro number = 6,023·10²³.
1 cm = 10⁻² m = 10⁻⁵ km.
Answer:
I think it's the second answer --If you increase the acidity..
I hope answer I can answer your question!
Answer:
2.2 moles of Fe will be produced
Explanation:
Step 1: Data given
Number of moles of hydrogen gas = 3.3 moles
Number of moles of iron oxide = 1.5 moles
Step 2: The balanced equation
3H2 + Fe2O3 → 2Fe + 3H2O
Step 3: Calculate the limiting reactant
For 3 moles H2 we need 1 mol Fe2O3 to produce 2 moles Fe and 3 moles H2O
Hydrogen gas is the limiting reactant. It will completely be consumed (3.3 moles). Fe2O3 is in excess. There will react 3.3 / 3 = 1.1 moles
There will remain 1.5 - 1.1 = 0.4 moles Fe2O3
Step 4: Calculate moles Fe
For 3 moles H2 we need 1 mol Fe2O3 to produce 2 moles Fe and 3 moles H2O
For 3.3 moles H2 we'll have 2/3 * 3.3 = 2.2 moles Fe
2.2 moles of Fe will be produced
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.
