Diethyl ether, since 20 is closer to 34.6 it should start boiling faster than the other which is no where near it
Answer:
The first one is air the second is decreases the third is water the fourth is gas and the last is liquid.
Explanation:
Hope it helps.
They will mold into different shapes
Answer:
- What is the AGⓇ of this reaction? 0.
- Which will be favoured - the forward reaction, the reverse reaction, or neither? Neither.
- What effect does the presence of the enzyme aspartate transaminase have on the Key value when compared with its value in the absence of enzyme? It does not affect the value of Keq.
- If one of the products of reaction 1, oxaloacetate, is removed by converting it to citrate as follows: Reaction 2: oxaloacetate + acetyl-CoA citrate + COASH will the key for Reaction l be changed? No, the Keq does not change.
Explanation:
1. To calculate the delta G of a reaction given the K, we use the following equation:
ΔG°= -RT ln K.
Which gives us 0 when K is 1.
2.None of the reactions is favoured. Given that the K equals 1, the system will try to keep the concentration of both products and reagents the same.
3. A catalyst is a substance that, when added, provides a different and faster mechanism through which a reaction takes place. This only means that the speed at which the equilibrium is attained is reduced, but the enzyme does nothing to alter the difference in energy (ΔG°) of the start and end points of the reaction, which ultimately gives us the value of Keq.
4. The addition of a side reaction does not change the value of Keq for the main reaction. They are both separate ways of making oxaloacetate disappear. While the Keq does not change, keep in mind that the end concentrations will not be the same, for any set of starting concentrations of your substances.
Answer:
Michaelis constant is known as km which is the substrate concentration that encourages the compound to work at half maximum velocity represented by Vmax/2. Michaelis constant is inversely related to the substrate and the affinity of the enzyme.
Induced fit model: The premise of the purported induced fit hypothesis, which expresses that the attachment or association of a substrate or some other atom to an enzyme causes an adjustment to the enzyme in order to fit or restrain its activity.
In substrate, analog Km or Michaelis constant will be high as the substrate will stay because of analogs inhibit activity.
In the transitional state, analog Km will be in the middle of the substrate and product analogs. Progress state analogs are synthetic mixes with a structure catalyzed reaction that looks like the progressing condition of a substrate atom in a compound enzyme.
In item simple thus Km is the least.
0.0013 M = product ananlog,
0.025 M=Transition state, and
0.0045 M = Substrate analog
