Answer:
The correct answer is 1 glycogen degradation would slow down.
Explanation:
Glycogen is the principle storage polysaccharide present in the liver and muscle of human body.
Glycogen contain both alpha-1,4-glycosidic linkage and alpha -1,6-glycosidic linkage.During glycogenolysis some glucose residues are transferred from branch point of the glycogen to its end and thereafter a single glucose residue is linked to the branch point of glycogen by alpha-1,6-glycosidic linkage.
The alpha-1,6-glycosidic linked glucose of glycogen is finally get separated from glycogen by the catalytic activity of alpha-1,6-glycosidase enzyme in the final step of glycogenolysis.
According to the given question if there is no alpha-1,6-glycosidic linkage in the glycogen then glycogen degradation will slow down.
Answer:
ΔH0reaction = [ΔHf0 CO2(g)] - [ΔHf0 CO(g) + ΔHf0 O2(g)]
Explanation:
Chemical equation:
CO + O₂ → CO₂
Balanced chemical equation:
2CO + O₂ → 2CO₂
The standard enthalpy for the formation of CO = -110.5 kj/mol
The standard enthalpy for the formation of O₂ = 0 kj/mol
The standard enthalpy for the formation of CO₂ = -393.5 kj/mol
Now we will put the values in equation:
ΔH0reaction = [ΔHf0 CO2(g)] - [ΔHf0 CO(g) + ΔHf0 O2(g)]
ΔH0reaction = [-393.5 kj/mol] - [-110.5 kj/mol + 0]
ΔH0reaction = [-393.5 kj/mol] - [-110.5 kj/mol]
ΔH0reaction = -283 kj/mol
Answer:
The answer will be Ligand A with a dissociation constant (Kd) of 
M
Explanation:
When the dissociation constant in the ligand is small (in order of nano) ( ) it will be more tied. Due to a dissociation constant measures how much a ligand can be able to be separated from the protein so if the number is small it means that the ligand is highly binded to the protein.
On the other hand, the occupancy percentage of the ligand does not imply binding. Conversely, a High-affinity ligand binding with the proteins implies that a relatively low concentration of a ligand is adequate to occupy the maximum ligand-binding site.
1 and 5 are definitely significant. The zeros might not be significant .
