Answer:
Around 17,000,000 or a little more than that
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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Answer:
0.25L
Explanation:
Using the dilution formula
C1V1=C2V2
C1=6M
V1?
C2=0.75M
V2=2.0L
V1= C2V2/C1
V1=0.75*2.0/6
V1=0.25L
Answer:
It kind of is logical so my answer is yes
Answer:
6. d
7.c
8.a
9.b
Explanation:
For 6, the answers are not particularly close to 100, and they are not clustered much. For 7, the answers are all clustered very close to 100. For 8, the answers are clustered closely, but not close to 100. For 9, the answers are close to 100, but not clustered very tightly. Hope this helps!
