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Rate of Protein Synthesis A bacterial ribosome can synthesize about 20 peptide bonds per minute. If the average bacterial protein is approximately 260 amino acid residues long, how many proteins can the ribosomes in an \(E\). coli cell synthesize in 20 minutes if all ribosomes are functioning at maximum rates?

Short Answer

Expert verified
Each ribosome can synthesize 1 complete protein in 20 minutes.

Step by step solution

01

Determine the Time for One Protein

First, calculate how long it takes to synthesize a single protein. With the synthesis rate of 20 peptide bonds per minute and a protein length of 260 amino acids, we can calculate the time needed to complete one protein:The time (in minutes) is calculated as:\[ \text{Time for one protein} = \frac{\text{Protein length}}{\text{Rate of synthesis}} = \frac{260}{20} \]Simplifying gives:\[ 13 \text{ minutes per protein} \]
02

Calculate Total Proteins in Given Time

Next, determine how many such proteins can be synthesized in the given time frame of 20 minutes. The formula to use is:\[ \text{Number of proteins} = \frac{\text{Total time available}}{\text{Time per protein}} = \frac{20}{13} \]Calculating gives approximately:\[ 1.54 \text{ proteins} \]
03

Interpret the Result

Since it is not possible to synthesize a fraction of a protein, we can conclude that each ribosome produces 1 complete protein in the given time.

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Key Concepts

These are the key concepts you need to understand to accurately answer the question.

Bacterial Ribosome
The bacterial ribosome plays a crucial role in the process of protein synthesis. It acts as the machinery where proteins are assembled, reading the genetic code and translating it into functional proteins. Each ribosome consists of two subunits, which come together to form the active site for protein synthesis.
Bacterial ribosomes are slightly smaller than eukaryotic ribosomes, with a sedimentation coefficient of 70S (Svedberg units), compared to the 80S found in eukaryotes.
  • The small subunit reads the mRNA sequence.
  • The large subunit links amino acids to form proteins.
Each component of the ribosome, proteins, and rRNA, plays a specific role in accurately translating the genetic code into a chain of amino acids.
The efficiency of ribosomes is critical in allowing bacterial cells, like those in *E. coli*, to adapt rapidly to environmental changes by quickly synthesizing necessary proteins.
Amino Acid Residues
Amino acid residues are the building blocks of proteins, which are synthesized by ribosomes. They link together in a specific sequence to form polypeptide chains.
These sequences determine the structure and function of the resulting protein. During protein synthesis, tRNA molecules bring amino acids to the ribosome, where they are added to the growing polypeptide chain.
  • There are 20 standard amino acids used in protein building.
  • Each has a unique side chain that affects protein folding and function.
The term "residue" refers to amino acids as they are incorporated into proteins, subtracting a water molecule through dehydration synthesis.
This condensation reaction is part of the formation of peptide bonds, the next step in developing a complete protein structure.
Peptide Bonds
Peptide bonds are the links that hold amino acids together, forming a polypeptide chain. These covalent chemical bonds connect the carboxyl group of one amino acid to the amino group of the next, releasing a water molecule in the process.
  • The creation of each peptide bond releases energy, aiding in protein folding.
  • They provide structural stability to proteins.
In bacterial ribosomes, peptide bond formation is catalyzed by an RNA molecule within the large ribosomal subunit, known as the peptidyl transferase center. This enzyme accelerates the reaction, allowing for rapid protein synthesis.
For example, in *E. coli*, these peptide connections enable fast growing conditions, vital for survival and adaptation.
E. coli
*E. coli* is a type of bacteria commonly found in the intestines of warm-blooded organisms. It is often used as a model organism in biotechnology and microbiology due to its rapid growth and ease of genetic manipulation.
This bacterium benefits from its efficient ribosomes, which can synthesize proteins quickly, allowing it to respond swiftly to changing environments.
  • *E. coli* cells typically reproduce quickly, often doubling every 20 minutes.
  • They are instrumental in studies of molecular biology and genetic engineering.
Understanding how *E. coli* ribosomes function gives insights into bacterial protein synthesis, helping us comprehend broader biological processes.
Additionally, because *E. coli* is well-studied, findings often translate to applications in medicine, such as antibiotic development and understanding bacterial resistance mechanisms.

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Most popular questions from this chapter

Effect of Single-Base Changes on Amino Acid Sequence Much important confirmatory evidence on the genetic code has come from assessing changes in the amino acid sequence of mutant proteins after a single base has been changed in the gene that encodes the protein. Which of the listed amino acid replacements would be consistent with the genetic code if the replacements were caused by a single base change? Which cannot be the result of a single- base mutation? Why? a. Phe \(\rightarrow\) Leu b. Lys \(\rightarrow\) Ala c. Ala \(\rightarrow\) Thr d. Phe \(\rightarrow\) Lys e. Ile \(\rightarrow\) Leu f. His \(\rightarrow\) Glu g. Pro \(\rightarrow\) Ser

The Genetic Code in Action Translate the mRNA shown, starting at the first 5 ' nucleotide, assuming that translation occurs in an \(E\). coli cell. If all tRNAs make maximum use of wobble rules but do not contain inosine, how many distinct tRNAs are required to translate this RNA? (5) AUGGGUCGUGAGUCAUCGUUAAU

The Genetic Code and Mutation A mutation occasionally arises that converts a codon specifying an amino acid to a stop or nonsense codon. When this occurs in the middle of a gene, the resulting protein is truncated and often inactive. If the protein is essential, cell death can result. Which of these secondary mutations might restore some or all of the protein function so that the cell can survive (there may be more than one correct answer)? a. A mutation restoring the codon to one encoding the original amino acid b. A mutation changing the nonsense codon to one encoding a different but similar amino acid c. A mutation in the anticodon of a tRNA such that the tRNA now recognizes the nonsense codon d. A mutation in which an additional nucleotide inserts just upstream of the nonsense codon, changing the reading frame so the nonsense codon is no longer read as "stop"

Proofreading by Aminoacyl-tRNA Synthetases The isoleucyl-tRNA synthetase has a proofreading function that ensures the fidelity of the aminoacylation reaction, but the histidyl-tRNA synthetase lacks such a proofreading function. Explain.

Predicting Anticodons from Codons Most amino acids have more than one codon and attach to more than one tRNA, each with a different anticodon. Write all possible anticodons for the four codons of glycine: \(\left(5^{\prime}\right) \mathrm{GGU}, \mathrm{GGC}\), GGA, and GGG. a. From your answer, which of the positions in the anticodons are primary determinants of their codon specificity in the case of glycine? b. Which of these anticodon-codon pairings has/have a wobbly base pair? c. In which of the anticodon-codon pairings do all three positions exhibit strong Watson-Crick hydrogen bonding?

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