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In a mixed copolymer experiment, messages were created with either \(4 / 5 \mathrm{C}: 1 / 5 \mathrm{A}\) or \(4 / 5 \mathrm{A}: 1 / 5 \mathrm{C}\). These messages yielded proteins with the amino acid compositions shown in the following table. Using these data, predict the most specific coding composition for each amino acid. $$\begin{array}{lccc} {}{} {4 / 5 \mathrm{C}: 1 / 5 \mathrm{A}} & {}{} {4 / 5 \mathrm{A}: 1 / 5 \mathrm{C}} \\ \text { Proline } & 63.0 \% & \text { Proline } & 3.5 \% \\ \text { Histidine } & 13.0 \% & \text { Histidine } & 3.0 \% \\ \text { Threonine } & 16.0 \% & \text { Threonine } & 16.6 \% \\ \text { Glutamine } & 3.0 \% & \text { Glutamine } & 13.0 \% \\ \text { Asparagine } & 3.0 \% & \text { Asparagine } & 13.0 \% \\ \text { Lysine } & \underline{0.5 \%} & \text { Lysine } & \underline{50.0 \%} \\\ & 98.5 \% & & 99.1 \% \end{array}$$

Short Answer

Expert verified
Answer: The predictions are as follows: - Proline: More reliant on C - Histidine: More reliant on C - Threonine: Evenly reliant on C and A - Glutamine: Evenly reliant on C and A - Asparagine: Evenly reliant on C and A - Lysine: More reliant on A

Step by step solution

01

Identify the amino acids with higher occurrence in each message

Compare the percentages of each amino acid in both messages: Message 1 (4/5 C: 1/5 A): Proline 63%, Histidine 13%, Threonine 16%, Glutamine 3%, Asparagine 3%, Lysine 0.5% Message 2 (4/5 A: 1/5 C): Proline 3.5%, Histidine 3%, Threonine 16.6%, Glutamine 13%, Asparagine 13%, Lysine 50% From the comparison, we can see that Proline and Histidine are much more prominent in message 1 compared to message 2, whereas Lysine is much more prominent in message 2 compared to message 1.
02

Determine the coding compositions based on nucleotide contribution

Since Proline and Histidine are more prominent in message 1, where C is more abundant, it is reasonable to infer that the coding composition for these amino acids is more reliant on C than on A. Similarly, because Lysine is much more prominent in message 2, where A is more abundant, it is likely that the coding composition for Lysine is more reliant on A than on C. Threonine, Glutamine, and Asparagine have roughly similar proportions in each message, indicating that their coding compositions are likely more evenly dependent on both C and A.
03

Predict the specific coding compositions for each amino acid

Based on the conclusions from Step 2, we can predict the most specific coding compositions for each amino acid: - Proline: More reliant on C - Histidine: More reliant on C - Threonine: Evenly reliant on C and A - Glutamine: Evenly reliant on C and A - Asparagine: Evenly reliant on C and A - Lysine: More reliant on A These predictions provide a rough estimate of the coding compositions for each amino acid in these messages; however, more detailed analysis or experimental data would be necessary to accurately determine individual nucleotide codes for each amino acid.

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Most popular questions from this chapter

Sydney Brenner argued that the code was nonoverlapping because he considered that coding restrictions would occur if it were overlapping. A second major argument against an overlapping code involved the effect of a single nucleotide change. In an overlapping code, how many adjacent amino acids would be affected by a point mutation? In a nonoverlapping code, how many amino acid(s) would be affected?

Suppose that in the use of polynucleotide phosphorylase, nucleotides A and C are added in a ratio of 1A:5C. What is the probability that an AAA sequence will occur?

An alanine residue exists at position 180 of a certain plant protein. If the codon specifying alanine is GCU, how many singlebase substitutions will result in an amino acid substitution at position \(180,\) and what are they?

A novel protein discovered in a certain plant has many leucinerich regions, fewer alanine-rich regions, and even fewer tyrosine residues. Correlate the number of codons for these three amino acids with this information.

One form of postranscriptional modification of most eukaryotic RNA transcripts is the addition of a poly-A sequence at the 3 '-end. The absence of a poly-A sequence leads to rapid degradation of the transcript. Poly-A sequences of various lengths are also added to many prokaryotic RNA transcripts where, instead of promoting stability, they enhance degradation. In both cases, RNA secondary structures, stabilizing proteins, or degrading enzymes interact with poly-A sequences. Considering the activities of RNAs, what might be the general functions of \(3^{\prime}\) -polyadenylation?

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