protein folding and structure

• What are the three main types of secondary structures in proteins?

  Alpha helices, beta sheets, and loops and coils
• What forces drive protein folding?

  Hydrophobic collapse, hydrogen bonds, ionic interactions, disulfide bridges
• What is the role of chaperone proteins in protein folding?

  They assist in proper protein folding
• What is the function of the proteosome?

  Degrades misfolded proteins
• What diseases are linked to misfolded proteins?


  Amyloidosis, Alzheimer’s, and prion diseases
• What is the definition of protein folding?

  Amino acid chains gain function by folding
• Why does protein folding occur within milliseconds?

  Due to thermodynamic stability and hydrophobic interactions
• What determines the biological function of a protein?

  The final structure after folding
• What is the primary structure of a protein?

  Linear sequence of amino acids
• What stabilizes peptide bonds in proteins?

  Partial double-bond character from delocalized electrons
• What does the Ramachandran plot display?

  Permissible ϕ and ψ angles based on steric clashes
• What forms the secondary structure of proteins?

  Hydrogen bonds between peptide backbone atoms
• How are alpha helices stabilized?

  By hydrogen bonds between specific amino acids
• What are beta sheets composed of?

  Beta strands linked by hydrogen bonds
• What characterizes loops and coils in protein structure?

  Flexible, irregular regions connecting secondary structures
• What defines the tertiary structure of a protein?

  The overall 3D shape formed by side-chain interactions
• What drives hydrophobic collapse in protein folding?

  Nonpolar amino acids forming a core, excluding water
• What are motifs in protein structure?

  Combinations of secondary structures
• What are domains in proteins?

  Independently folding, stable structural units
• What is the quaternary structure of a protein?

  Complex of multiple protein subunits
• What are homomers and heteromers?

  Homomers have identical subunits; heteromers have different subunits
• What is Levinthal’s Paradox?

  Random folding takes longer than the universe's age
• What does the folding funnel model describe?

  Proteins reach the lowest Gibbs free energy state
• How do chaperone proteins assist in protein folding?

  By preventing aggregation and resolving misfolded states
• What is the role of the proteosome in protein quality control?

  Degrades unwanted or misfolded proteins
• What are the consequences of protein misfolding?

  Aggregation leads to diseases like Alzheimer’s
• What is amyloidosis?

  Aggregation of amyloid fibrils in tissues
• What are prion diseases caused by?

  Misfolded prions catalyzing misfolding in normal proteins
• What is AlphaFold?

  AI-based system predicting 3D protein structures
• What are the applications of AlphaFold?

  Drug discovery, understanding mutations, solving structures
• What are the key takeaways regarding protein folding?

  • Protein folding is hierarchical and stepwise.
  • Misfolding disrupts function and leads to diseases.
  • Chaperones and proteosomes maintain protein quality.
  • Domains enable multifunctional properties in proteins.