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Answer:
The temperature of the gas is 876.69 Kelvin
Explanation:
Ideal gases are a simplification of real gases that is done to study them more easily. It is considered to be formed by point particles, do not interact with each other and move randomly. It is also considered that the molecules of an ideal gas, in themselves, do not occupy any volume.
The pressure, P, the temperature, T, and the volume, V, of an ideal gas, are related by a simple formula called the ideal gas law:
P*V = n*R*T
where P is the gas pressure, V is the volume that occupies, T is its temperature, R is the ideal gas constant, and n is the number of moles of the gas.
In this case:
- P= 470 mmHg
- V= 570 mL= 0.570 L
- n= 0.216 g= 0.0049 moles (being the molar mass of carbon dioxide is 44 g/mole)
- R= 62.36367
Replacing:
470 mmHg*0.570 L= 0.0049 moles* 62.36367 *T
Solving:
T= 876.69 K
<em><u>The temperature of the gas is 876.69 Kelvin</u></em>
Answer:
1) correct
2) incorrect
3) correct
4)incorrect
Explanation:
1) A Lewis acid is a substance that accepts a nonbonding pair of electrons.
A Bronsted-Lowry acid is a substance that donates a proton H⁺
Since the donation of a proton involves the acceptance of a pair of electrons, every Bronsted-Lowry acid is also a Lewis acid.
2)A Lewis acid not necessarily needs to have a proton to be donated.
3) Conjugated acids of weak bases are strong acids and conjugated acids of strong bases are weak acids.
4)K⁺ comes from a strong base, therefore is does not have an acidic behaviour.
<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.
