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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Divide velocity by the wavelength.
Answer:
People can introduce their own biases into an experiment.
Explanation:
Answer:
The answer is "Option D".
Explanation:
The behavior of 0.1M NaCl also isn't substantially larger objectively than those of 0.05M NaCl because a p-value above 0.05 (p>0.05) indicates no ability to tell differential and is a strong proof in favor of a null hypothesis.
The other wrong choices can be defined as follows:
- Option A as it's just the reverse of the correct answer to the null.
- Options B and C because p worth tests to support nor oppose the null hypothesis.
