The halogens are five non-metallic elements found in group 17 of the periodic table. The term "halogen" means "salt-former" and compounds containing halogens are called "salts". All halogens have 7 electrons in their outer shells, giving them an oxidation number of -1.
Answer: 22g of chlorine would be needed to carry out this synthesis reaction
Explanation:
A synthesis reaction is one in which two or more than two elements combine together to forma single product.
The atoms present in the reactants are found on the product side. According to the law of conservation of mass, the number of atoms on both sides of the arrow must be same as the total mass must be conserved.
15 grams of sodium reacts with 22 grams of chlorine to yield 37 grams of sodium chloride. Thus 22g of chlorine would be needed to carry out this synthesis reaction.
The answer is a, because the population number has increased.
Answer:
37.25 grams/L.
Explanation:
- Molarity (M) is defined as the no. of moles of solute dissolved per 1.0 L of the solution.
<em>M = (no. of moles of KCl)/(volume of the solution (L))</em>
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∵ no. of moles of KCl = (mass of KCl)/(molar mass of KCl)
∴ M = [(mass of KCl)/(molar mass of KCl)]/(volume of the solution (L))
∴ (mass of KCl)/(volume of the solution (L)) = (M)*(molar mass of KCl) = (0.5 M)*(74.5 g/mol) = 37.25 g/L.
<em>So, the grams/L of KCl = 37.25 grams/L.</em>
<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.
