Answer:
The cis double bond present in unsaturated fatty acids acids results in lower melting point when compared to saturated fatty acids of the same chain length.
Explanation:
Melting point of a fatty acids are affected by the length and degree of unsaturation of the hydrocarbon chain.
At room temperature, saturated fatty acids with hydrocarbon chain lengths between 12-24 are waxy solids whereas unsaturated atty acids of the same chain length are liquids. This is due to the nature of the packing of the fatty acid molecules in the saturated and unsaturated compounds.
In the saturated compounds, the molecules are tightly packed side by side with minimal steric hindrance and maximal van der Waals forces of attraction between molecules. However, in unsaturated fatty acids, the cis double bond introduces a bend or kink in the molecules which then interferes with the tight packing of the molecules and reducing interaction between molecules. Therefore, less energy is required to cause a disorder in the arrangement of unsaturated fatty acids, leading to a lowering of melting point.
Answer:
The atoms have the same chemical symbol.
Here are the resonance contributors I found.
Answer:
449 (g K) / 39.1 (g/mol K) = 11.5 mol K
Explanation:
Potassium has atomic number 39.1
amount of K in 449g sample = 449/39.1 = 11.5 mol
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:
