hi <3
changes in the enzyme's shape would decrease its ability to function as this would change the active site of the enzyme, meaning it is harder for it to carry out its job.
this is why we try to keep enzymes in their optimum environmental conditions so they can function their best
hope this helps :)
Answer:
A to N
Explanation:
Glutamine is an amino acid with a polar, uncharged side chain. The mutation to alanine, an amino acid with a non-polar side chain, completely affects the enzymatic activity. This makes sense considering the difference in the nature of both amino acids.
To restore the wild-type level of activity the alanine would have to mutate to another polar uncharged amino acid. Among the given options, only Asparagine (N) has a similar chemistry to Glutamine.
<span>The answer would be: Continue patient care by getting a complete SAMPLE history and perform a complete secondary assessment.
If the reading of glucose test is normal, then you can exclude hypoglycemia from the possible diagnosis. Because the patient is accompanied by his mother, you can ask a brief history to exclude other possible diagnosis and complete secondary assessment before further help comes. The information would be beneficial to the healthcare personnel that will comes for help.
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Nonliving characteristics include the fact that they are not cells, have no cytoplasm or cellular organelles, and carry out no metabolism on their own and therefore must replicate using the host cell's metabolic machinery. Viruses can infect animals, plants, and even other microorganisms.
