Hey there !
Number of moles of solution: 4.3 moles
Volume in liters:
450.0 mL / 1000 => 0.45 L
Therefore:
Molarity = number of moles / volume of solution ( L)
Molarity = 4.3 / 0.45
=> 9.55 M
Hope that helps!
Alkali metals are known for being some of the most reactive metals. This is due in part to their larger atomic radii and low ionization energies. They tend to donate their electrons in reactions and often have an oxidation state of +1. These metals are characterized as being extre
First write the molecular equation with states:
(NH4)2S (aq) + 2AgNO3(aq) → Ag2S (s) + 2NH4NO3
Now write a full ionic equation by separating into ions all substances that dissociate: anything (s) (g) or (l) does not dissociate
2NH4 + (aq) + S 2-(aq) + 2Ag+ (aq) + 2NO3- (aq) → Ag2S(s) + 2NH4 + (aq) + 2NO3- (aq)
To write the NET IONIC equation, inspect the full ionic equation above and delete anything that appears on both sides of the → sign:
Net ionic equation:
S 2-(aq) + 2Ag + (aq) → Ag2S(s)
Answer:
The answer is 130.953 g of hydrogen gas.
Explanation:
Hydrogen gas is formed by two atoms of hydrogen (H), so its molecular formula is H₂. We can calculate is molecular weight as the product of the molar mass of H (1.008 g/mol):
Molecular weight H₂= molar mass of H x 2= 1.008 g/mol x 2= 2.01568 g
Finally, we obtain the number of mol of H₂ there is in the produced gas mass (264 g) by using the molecular weight as follows:
mass= 264 g x 1 mol H₂/2.01568 g= 130.9731703 g
The final mass rounded to 3 significant digits is 130.973 g
<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.
