Answer:
The answer is rather simple, if you understand electron configurations: the shape of the periodic table mimics the filling of the subshells with electrons. The shape of the periodic table mimics the filling of the subshells with electrons. ... The next two electrons, for Li and Be, would go into the 2s subshell.
Explanation:
Answer:
Explanation:
If the enzyme active site is complementary to the substrate conformation rather than to the transition state, it is unlikely that the reaction will proceed and release a product, because the enzyme-substrate complex will be tightly bound (ΔG will raise).
On the other hand, when the enzyme active site is complementary to the transition state, the substrate will not be tightly bound and will be more prone to be transformed into the product (<u>ΔG will be lowered</u>) and afterward, be released.
The weak interactions (non-covalent bonds) will stabilize the energy of the transition state and reduce its energy, thus lowering the activation energy). If the transition state is stable, it will form more easily and<u> the reaction will be more likely to proceed.</u>
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False. Eyeglasses do not cover all around the eye however safety goggles do
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.
