Answer:
The correct answer is m= mol solute kg soivent
Explanation:
Molality is a measure of concentration, which indicates the moles of solute (in this case sodium hydroxide) in 1kg of solvent .
In this case:
0,800 kg water-----0,400 mol NaOH
1 ,000 kg water ---x=(1 ,000 kg water x 0,400 mol NaOH)/0,800 kg water
x=0,5 mol NaOH---> <em>The solution is 0,5 molal (0,5 m)</em>
I believe the answer is 0.016. if i am wrong please tell me if it's wrong. the second option
Answer:
- Increased volume of particles in the container
- greater vibration of particles
Explanation:
At higher temperature, the particles of the gas would be more active and vibrate more, or even have greater collisions. Alex can indicate this in the altered model to depict higher temperature.
Consequently, Charles law gives meaning to why there would be an increased volume of gas in the stable pressurized container, if the temperature were to be increased.
I hope this explanation was clear and concise?
Answer:
d. A competitive inhibitor, collect kinetic daa both in the presence and absence of inhibitor and watch for a change in Km.
Explanation:
According to the description, the inhibitor was designed in a way when it binds the enzyme, the transition state achieved will be close to the one observed when the substrate binds.
In other words, the aim was to design an inhibitor that will bind the free enzyme in a reversible way, competing with the substrate for the binding sites.
As the inhibitor will be binding the same site as the substrate, the apparent affinity of the enzyme for the substrate will decrease. And the higher the affinity of the inhibitor for the enzyme, stronger the effect it will have over the affinity of the enzyme for the substrate.
Quantitatively speaking, the apparent Km of the enzyme for the substrate will increase with the inhibitor concentration, as the affinity of the enzyme for the substrate decreases.
In summary, what is being engineered is a competitive inhibitor, and the way of knowing if the design was successful, is collecting kinetic data in presence and absence of inhibitor, and watch for changes in the apparent Km.
