<em>Answer:</em>
- At 60 centigrade, the kinetic energy of the substance will be greatest.
<em>Explanation:</em>
As we know, the kinetic energy of substance is directly proportional to Temperature.
The total Kinetic energy can be calculated as follow
K.E = 3/2 n.R.T
From the equations, it is cleared that Temperature is directly proportional to temperature.
Answer:
Final temperature: 659.8ºC
Expansion work: 3*75=225 kJ
Internal energy change: 275 kJ
Explanation:
First, considering both initial and final states, write the energy balance:
Q is the only variable known. To determine the work, it is possible to consider the reversible process; the work done on a expansion reversible process may be calculated as:
The pressure is constant, so: 
(There is a multiplication by 100 due to the conversion of bar to kPa)
So, the internal energy change may be calculated from the energy balance (don't forget to multiply by the mass):
On the other hand, due to the low pressure the ideal gas law may be appropriate. The ideal gas law is written for both states:
Subtracting the first from the second:
Isolating 
:
Assuming that it is water steam, n=0.1666 kmol
ºC
Answer:
The products are CO₂ and H₂O.
The ballanced equation is this:
2C₄H₆ + 11O₂ → 8CO₂ + 6H₂O
Explanation:
In any chemical reaction, where you see that you have a compound reacting only with oxygen (O₂), you are in front of combustion.
Products in combustion are always water vapor and carbon dioxide.
Take a look to the methane combustion.
CH₄ + 2O₂ → CO₂ + 2H₂O
1 mol of methane reacts with 2 moles of oxygen to form 1 mol of CO₂ and 2 moles of water.
This is the combustion for an alkene where 2 moles of the alkene reacts with 11 moles of oxygen to make water and CO₂ like this:
2C₄H₆ + 11O₂ → 8CO₂ + 6H₂O
Explanation:
mg 2+ losses 2 electron due to the charge on it making it change from 12 to 10.and ne is also 10
Answer:
A inhibitor structure resembles substrate structure B inhibitor binds non covalently at site other than active site.C inhibitors bind covalently and permanently at active site.
Explanation:
A Reversible competitive inhibitors structurally resembles the substrate and competes with the substrate to bind to the active site of the target enzyme.
B Reversible noncompetitive inhibitors binds no covalently at site of the target enzyme that is different from the active site.
C irreversible inhibitors interacts very tightly to the active site of an enzyme by covalent bond which cannot be overcome.
