Answer:
False
Explanation:
False. The molecules of liquid are hold in the liquid state due to intermolecular forces or Van de Waals forces , without affecting the molecule itself and its atomic bonds (covalent bonds). When the temperature increases the kinetic energy of the molecules is higher , therefore they have more possibilities to escape from the attractive intermolecular forces and go to the gas state.
Note however that this is caused because the intermolecular forces are really weak compared to covalent bonds, therefore is easier to break the first one first and go to the gas state before any covalent bond breaks ( if it happens).
A temperature increase can increase vaporisation rate if any reaction is triggered that decomposes the liquid into more volatile compounds , but nevertheless, this effect is generally insignificant compared with the effect that temperature has in vaporisation due to Van der Waals forces.
Answer:
The area around the nucleus must be of low mass.
Explanation:
Rutherford`s experiment showed that there are some positive charges in the center of the atoms, and because they are all together, they will give a great mass to the atom.
It was quite different from Thomson`s experiment, in which it was thought that the negative charges were mixed with the positive charges, around the atom (like a Pudding Model). In Rutherford`s experiment, because the direction of beta particles, it was the prediction of the positive nucleus.
Hope this info is useful.
Answer:
c. By itself, heme is not a good oxygen carrier. It must be part of a larger protein to prevent oxidation of the iron.
e. Both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a central iron ( Fe ) (Fe) atom.
f. Hemoglobin is a heterotetramer, whereas myoglobin is a monomer. The heme prosthetic group is entirely buried within myoglobin.
Explanation:
The differences between hemoglobin and myoglobin are most important at the level of quaternary structure. Hemoglobin is a tetramer composed of two each of two types of closely related subunits, alpha and beta. Myoglobin is a monomer (so it doesn't have a quaternary structure at all). Myoglobin binds oxygen more tightly than does hemoglobin. This difference in binding energy reflects the movement of oxygen from the bloodstream to the cells, from hemoglobin to myoglobin.
Myoglobin binds oxygen
The binding of O 2 to myoglobin is a simple equilibrium reaction:
I think it’s A but I’m not sure, if it’s wrong I’m sorry
