Complete question:
ΔU for a van der Waals gas increases by 475 J in an expansion process, and the magnitude of w is 93.0 J. calculate the magnitude of q for the process.
Answer:
The magnitude of q for the process 568 J.
Explanation:
Given;
change in internal energy of the gas, ΔU = 475 J
work done by the gas, w = 93 J
heat added to the system, = q
During gas expansion process, heat is added to the gas.
Apply the first law of thermodynamic to determine the magnitude of heat added to the gas.
ΔU = q - w
q = ΔU + w
q = 475 J + 93 J
q = 568 J
Therefore, the magnitude of q for the process 568 J.
Answer:
A. It formed by barium(Ba+2) ion and sulfate ( SO42- )
B. It is formed by calcium ion (Ca+2) and two fluoride ions (2F-)
C. It is formed by magnesium ion (Mg+2) and nitride ion (N3-)
D. It is formed by two potassium ions (2 K+) and oxide ion(O2-)
Explanation:
it should be option number (D) Iron (III) oxide
Consequences of oxygenation. Eventually, oxygen started to accumulate in the atmosphere, with two major consequences. Oxygen likely oxidized atmospheric methane (a strong greenhouse gas) to carbon dioxide (a weaker one) and water.
<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.
