Biology: Amino Acids and Proteins

Choose a study mode

Play Quiz
Study Flashcards
Spaced Repetition
Chat to Lesson

Podcast

Play an AI-generated podcast conversation about this lesson

Questions and Answers

Which of the following best describes phenylalanine?

  • A branched-chain amino acid
  • Contains a sulfhydryl group
  • Contains a hydroxyl group
  • An aromatic amino acid (correct)
  • A dietary nonessential amino acid

Which of the following amino acids is most likely a precursor of the neurotransmitter GABA?

  • Aspartate
  • Tryptophan
  • Glutamine
  • Glutamate (correct)
  • Tyrosine
  • Glycine

A researcher is studying the secondary structure of an enzyme involved in intermediary metabolism. He observes that it contains alpha-helices. Which of the following best describes this structure?

  • A structure favored by a high amount of proline residues
  • Stabilized by peptide bonds
  • Contains amino acids with their side chains towards the outside of the helix (correct)
  • Retained when the protein is heated to high temperatures
  • Stabilized by phosphodiester linkages

A research group is studying covalent bonds which are formed by the side chains of amino acids. Which of the following bonds is most likely being studied by this research group?

<p>Disulfide bonds between two cysteine residues (A)</p> Signup and view all the answers

Which of the following best describes gene expression in bacteria?

<p>Some internal AUG sequences must be recognized as start codons (B)</p> Signup and view all the answers

Which of the following positions best indicates the first nucleotide of the anticodon?

<p>5 (D)</p> Signup and view all the answers

A research laboratory studies a disease-causing gene that leads to loss of function of an enzyme in a metabolic pathway. Karyotyping and DNA microarray shows that the chromosome structure is unchanged. Northern blot analysis shows no change in the mRNA transcript of the gene. Western blot shows a smaller than normal protein is formed.

<p>One base pair insertion in an exon (B)</p> Signup and view all the answers

Which of the following modifications is most likely observed during the process of primary insulin translation product undergoing modifications to produce the mature insulin hormone?

<p>Hydrolytic cleavage of specific peptide bonds (E)</p> Signup and view all the answers

A researcher has developed a bacterial strain in the laboratory with reduced rates of translation. It has a mutation which confers decreased activity in peptide bond formation during ribosomal protein synthesis. A Mutation in which of the following is most consistent with these findings?

<p>One of the ribosomal RNAs (A)</p> Signup and view all the answers

Which of the following codon changes best explains the loss of an important alpha-helical segment of the protein?

<p>CUC to CCC (A)</p> Signup and view all the answers

Which of the properties of the code in the novel organism is most likely different from the terrestrial (earth) genetic code?

<p>The genetic code was overlapping (D)</p> Signup and view all the answers

Which of the following processes is most likely inhibited by the antibiotic erythromycin?

<p>The translocation step of translation in bacteria (D)</p> Signup and view all the answers

Flashcards

Phenylalanine

An aromatic amino acid that is essential in diet.

GABA precursor

Glutamate can be decarboxylated to form GABA.

Alpha-helix

A secondary structure of proteins stabilized by hydrogen bonds.

Covalent bond in proteins

Disulfide bonds formed between cysteine side chains.

Signup and view all the flashcards

Polycistronic mRNA

A single mRNA that encodes multiple enzymes in bacteria.

Signup and view all the flashcards

Anticodon

The tRNA region that pairs with mRNA codons during translation.

Signup and view all the flashcards

Mutation effects on mRNA

Insertions in exons may not change mRNA structure.

Signup and view all the flashcards

Insulin modification

Involves hydrolytic cleavage to become functional insulin.

Signup and view all the flashcards

Translation inhibition by erythromycin

Inhibits translocation during peptide synthesis in bacteria.

Signup and view all the flashcards

Codon usage

Different codons can code for the same amino acid (degeneracy).

Signup and view all the flashcards

Overlapping genetic code

A characteristic likely different in the Martian organisms.

Signup and view all the flashcards

Ribosomal RNA function

Catalytic RNA that facilitates peptide bond formation.

Signup and view all the flashcards

Hydrophobic interactions

Noncovalent forces driving hydrophobic amino acids together.

Signup and view all the flashcards

Signal peptide

Leads to the cleavage for mature protein synthesis.

Signup and view all the flashcards

Frameshift mutation

Caused by base pair insertion or deletion leading to altered reading frame.

Signup and view all the flashcards

Degenerate codons

Multiple codons that specify the same amino acid.

Signup and view all the flashcards

Transcription inhibitors

Compounds that prevent mRNA synthesis from DNA.

Signup and view all the flashcards

Chorismate

Intermediate in the synthesis pathways for certain amino acids.

Signup and view all the flashcards

Disulfide bond

Covalent bond formed between sulfur atoms in cysteine residues.

Signup and view all the flashcards

Polypeptide modifications

Post-translational alterations that affect final protein form.

Signup and view all the flashcards

Ribosomal protein synthesis

Process involving elongation factors during translation.

Signup and view all the flashcards

Eukaryotic vs prokaryotic translation

Bacteria have formyl-methionine; eukaryotes use methionine.

Signup and view all the flashcards

Gene expression regulation

Control over the transcription and translation of genes.

Signup and view all the flashcards

Protein denaturation

Loss of protein structure due to heat or pH changes.

Signup and view all the flashcards

AUG start codon

Initiates protein synthesis by providing methionine.

Signup and view all the flashcards

Amino acid side chains

Determine the properties and function of proteins.

Signup and view all the flashcards

Study Notes

Practice Questions: Translation, Amino Acids, and Proteins

  • Question 1: Aspartame, an artificial dipeptide sweetener, contains phenylalanine. Phenylalanine is an aromatic amino acid.

  • Question 2: GABA (gamma-aminobutyric acid) is formed by decarboxylating glutamate.

  • Question 3: Enzyme secondary structure, specifically alpha-helices, is stabilized by hydrogen bonds. R-groups face outwards in alpha-helices.

  • Question 4: Covalent bonds in tertiary protein structure are most likely formed by disulfide bonds between cysteine residues.

  • Question 5: E. coli gene expression for tryptophan synthesis is polycistronic, meaning one mRNA will produce multiple enzymes.

Further Questions and Explanations

  • Question 6: Figure indicates the first nucleotide of the anticodon is position 5.

  • Question 7: A smaller-than-normal protein, unchanged mRNA transcript, and unchanged chromosome, suggests a base-pair insertion within an exon.

  • Question 8: Insulin modifications after synthesis include peptide bond cleavage.

  • Question 9: Reduced rates of translation are consistent with mutations in ribosomal proteins or ribosomal RNA.

  • Question 10: A codon change from CUC to CCC (results in an altered amino acid) would cause a loss of an important alpha-helical segment.

  • Question 11: The Martian code likely differs in the amino acid that is assigned to certain codons from terrestrial genetic codes.

  • Question 12: Erythromycin inhibits bacterial protein synthesis at the translocation step of elongation.

  • Additional Practice Questions: The indicated pages in Lippincott's Biochemistry textbook provide more practice questions covering DNA structure and replication, RNA structure, synthesis, and processing.

Studying That Suits You

Use AI to generate personalized quizzes and flashcards to suit your learning preferences.

Quiz Team
Use Quizgecko on...
Browser
Browser