1.D 2.A that is pretty hard
Answer:
c. By itself, heme is not a good oxygen carrier. It must be part of a larger protein to prevent oxidation of the iron.
e. Both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a central iron ( Fe ) (Fe) atom.
f. Hemoglobin is a heterotetramer, whereas myoglobin is a monomer. The heme prosthetic group is entirely buried within myoglobin.
Explanation:
The differences between hemoglobin and myoglobin are most important at the level of quaternary structure. Hemoglobin is a tetramer composed of two each of two types of closely related subunits, alpha and beta. Myoglobin is a monomer (so it doesn't have a quaternary structure at all). Myoglobin binds oxygen more tightly than does hemoglobin. This difference in binding energy reflects the movement of oxygen from the bloodstream to the cells, from hemoglobin to myoglobin.
Myoglobin binds oxygen
The binding of O 2 to myoglobin is a simple equilibrium reaction:
Is A “the density of the ice decreased as it melted”
The nurse<span> is </span>caring<span> for a </span>client<span> with a temperature of 104.5 degrees Fahrenheit. A health </span>care provider<span> prescribes 500 mg of an antibiotic intravenous While undergoing a soapsuds </span>enema, theclient reports abdominal<span> cramping.</span>
Answer:
Uranium-238 undergoes alpha decay to form Thorium-234 as daughter product.
Explanation:
Alpha decay is indicative of loss of the equivalents of a helium particle emission. The reaction equation for this reaction is shown below:
→ 
I hope this explanation is clear and explanatory.
