Each element is diffrent than another element
Answer:
1.3 M.
Explanation:
- We need to calculate the mass of the solution:
mass of the solution = mass of MgCl₂ + mass of water
mass of MgCl₂ = 20.1 g.
mass of water = d.V = (157.0 mL)(1.0 g/cm³) = 157.0 g.
∴ mass of the solution = mass of MgCl₂ + mass of water = 20.1 g + 157.0 g = 177.1 g.
- Now, we can get the volume of the solution:
V of the solution = (mass of the solution)/(density of the solution) = (177.1 g)/(1.089 g/cm³) = 162.62 mL = 0.163 L.
Molarity is the no. of moles of solute dissolved in a 1.0 L of the solution.
M = (no. of moles of MgCl₂) / (Volume of the solution (L)).
<em>∴ M = (mass/molar mass)of MgCl₂ / (Volume of the solution (L)) =</em> (20.1 g/95.211 g/mol) / (0.163 L) = <em>1.29 M ≅ 1.3 M.</em>
Answer:
Acknowledge the source of relative weight of titanium.
Explanation:
Titanium is a chemical element which durable form of metal. Titanium is 45% lighter than steel. Titanium is made by combination of multiple elements. Titanium is very difficult to extract and this is the reason this element is considered expensive. The students examining the titanium must record the weight of titanium before exploring the characteristics and properties.
Explanation:
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<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.
