Answer:
Explanation:
A. The charge on an element is determined by the differences between the number of protons and electrons in an atom.
An atom will have no charges if the number of protons and electrons are the same.
- When an atom loses or gains electrons, the number of electrons will either decrease or increase
- if the number of electrons is more than the number of protons, the excess electrons is the charge on the atom. And this makes the atom become a negatively charged ion.
- if the number of electrons is lesser than the number of protons, the deficient electrons makes the atom a positively charged ion. The number of electrons by which the atom is deficient makes the atom a positively charged ion.
Charge = number of protons - number of electrons
B. Electrons form the charges they do because with the charge, they become stable like the noble gases.
The desire of every atom is to have stable electronic configuration like those of the noble gases.
A potassium atom with a configuration 2 8 8 1 will prefer to lose an electron to become an Argon atom making the ion stable.
I believe that the choices for this question are:
C2H4O2, C4H8O4 CH2O, C6H12O6 C3H6O3, C6H12O6 C2H4O2, C6H12O6
The answer to this based on the molar masses given is:
C2H4O2, C6H12O6
To prove calculate the molar mass:
C2H4O2 = 2*12 + 4*1 + 2*16 = 60
C6H12O6 = 6*12 + 12*1 + 6*16 = 180
<h3><u>Answer;</u></h3>
The statements that are True are;
- Upon binding a molecule of oxygen, Hb undergoes a conformational change that makes the binding of subsequent O2 molecules easier.
- The conformational change induced in Hb upon binding oxygen is the result of a small movement (0.2 Å) of the iron cation in the center of heme.
- Site-directed mutagenesis studies have indicated that the cooperativity of O2 binding in Hb is attributable to the movement of the F helix in Hb.
<h3><u>Explanation</u>;</h3>
- Hemoglobin is a key pigment in the blood that transports oxygen gas to all the tissues in the body. It is made up of two types of chains; that is two alpha chains and two beta chains.
- in its deoxygenated state hemoglobin has a low affinity for oxygen compared to myoglobin. When oxygen is bound to the first subunit of hemoglobin it leads to subtle changes to the quaternary structure of the protein. This in turn makes it easier for a subsequent molecule of oxygen to bind to the next subunit.
Answer:
It is liquid at most temperatures on Earth.