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frutty [35]
3 years ago
7

Suppose that a glutamine residue in the active site of an enzyme was mutated to alanine. As expected, the alanine mutant was ina

ctive, suggesting that the glutamine residue was critical to the catalytic mechanism. Which mutation is most likely to restore wild-type level of activity to the alanine mutant?
A to M

A to N

A to F

A to K

A to E
Biology
1 answer:
likoan [24]3 years ago
7 0

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.

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"The Introduction section of a scientific research article provides detailed information regarding the experimental design of th
Arisa [49]

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7 0
3 years ago
Suppose the frameshift mutation was still present, but now there was a base substitution (A to C) in the arginine (R) codon, cha
maksim [4K]

Answer:

A. The rest is still out of frame

Explanation:

The mRNA codon translated to amino acids is placed below.

While serine, which is one of the amino acids in the original protein, is still there as a part of the new sequence, there are a host of other frame shift mutations. While it is possible to phosphorylate a serine in any of these amino acid sequences, the secondary and tertiary structure of these are different to each other.

Original:

5' - UG | GUC | GGC | GAG | AAC | GAA | AGC | GC - 3'  

              Val     Gly      Glu      Asn     Glu      Ser

Mutation:

5' - UG | GUC | GGG | AGC | ACG | AAA | GCG | C - 3'

              Val      Gly      Ser      Thr     Lys      Ala      

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