Protein Cycle: Translation, Folding, Processing
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Questions and Answers

What is the function of a chaperone in the protein cycle after translation?

  • Removing unneeded polypeptides
  • Assisting in the folding of the polypeptide into its native conformation (correct)
  • Attaching fatty acid molecules to the polypeptide
  • Translocating the modified peptide to a membrane

What process involves attaching several ubiquitin molecules to a protein?

  • Covalent modification
  • Activation/Catalysis
  • Folding/Refolding
  • Degradation (correct)

What can trigger an enzyme to adopt a catalytically active conformation?

  • Binding an allosteric effector (correct)
  • Translocation to a membrane
  • Ribosome synthesis
  • Aging

Which event is most likely to occur during the processing phase of the protein cycle?

<p>Formation of disulfide bonds (A)</p> Signup and view all the answers

What happens during the degradation phase of the protein cycle?

<p>Degradation to amino acids for new protein synthesis (C)</p> Signup and view all the answers

What determines the tertiary structure of a protein?

<p>Sequence of amino acids in the chain (A)</p> Signup and view all the answers

What is the primary factor in favoring the formation of alpha helices?

<p>DELIMA amino acids (A)</p> Signup and view all the answers

Which type of protein has a structure that is nearly entirely a-helical?

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

How is a beta-pleated sheet stabilized?

<p>H-bonding between amide N's and carbonyl C's (D)</p> Signup and view all the answers

What defines the secondary structure of a protein?

<p>Sequence of amino acids forming intramolecular bonds (B)</p> Signup and view all the answers

Study Notes

Protein Cycle

  • Translation: synthesis of a polypeptide chain on a ribosome (RER) with its primary structure determined by an mRNA template
  • Folding/Refolding: nascent polypeptide folds into its native conformation with the assistance of chaperones to prevent misfolding

Processing

  • Accompanied by processing events such as:
    • Proteolytic cleavage of an N-terminal leader sequence
    • Formation of disulfide bonds (S-S)

Covalent Modification

  • Removing unneeded polypeptides
  • Attaching a fatty acid molecule, for example

Translocation

  • Modified peptide is translocated to a membrane
  • Examples: hemoglobin for the circulatory system

Activation/Catalysis

  • Binding an allosteric effector triggers a catalytically active conformation
  • Enzymes are involved in this step

Aging

  • Proteins become damaged by chemical attacks, deamidation, or denaturation

Ubiquitination

  • Proteins may be labeled by the covalent attachment of several ubiquitin molecules (Ub)

Degradation

  • Ubiquitinated protein is degraded to its component amino acids (reused for new protein synthesis)
  • Proteasome is involved in this step

Four Levels of Protein Structure

  • Primary Structure: sequence of amino acids and disulfide links
  • Secondary Structure: formed by hydrogen bonding, examples: alpha helix and beta-pleated sheet
  • Tertiary Structure: complete 3-D conformation of a protein
  • Quaternary Structure: association of two or more polypeptide chains

Protein Structure Examples

  • Alpha Helix:
    • Produces a helical coiling of the peptide backbone
    • R-groups lie on the exterior of the helix and perpendicular to its axis
    • Approximately 11 amino acids long (3.6 per complete turn)
    • DELIMA (amino acids) favor alpha helix formation
    • GP favors disruption of the helix
  • Beta-Pleated Sheet (B-Sheet):
    • Composed of 2 or more regions of stretches of at least 5-10 amino acids
    • Stabilized by H-bonding between amide N's and carbonyl C's
    • Found in both fibrous and globular proteins

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Description

This quiz covers the protein cycle involving translation on a ribosome, folding with the help of chaperones, and processing events like proteolytic cleavage. Test your knowledge on how polypeptides are synthesized, folded, and processed during protein synthesis.

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