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Protein Folding quiz #1 Flashcards

Protein Folding quiz #1
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  • What is the primary driving force behind the folding of proteins, and how does it influence the distribution of amino acids within the protein structure?
    The primary driving force behind protein folding is the hydrophobic effect, which causes non-polar (hydrophobic) amino acids to cluster in the protein's interior, away from water, while polar and charged (hydrophilic) amino acids are positioned on the protein's surface to interact with the aqueous environment.
  • How does Leventhal's paradox challenge the idea that protein folding is a random process, and what does it reveal about the nature of protein folding pathways?
    Leventhal's paradox demonstrates that protein folding cannot be a random process because testing all possible conformations would take longer than the age of the universe. Instead, proteins fold rapidly (in less than one second) by following predictable, cooperative folding pathways dictated by interactions among amino acids.
  • Where are charged, polar, and non-polar amino acids most likely to be found in a folded protein, and why?
    In a folded protein, non-polar (hydrophobic) amino acids are typically found in the interior, charged (hydrophilic) amino acids are found on the surface, and polar (but uncharged) amino acids can be found both on the surface and inside, due to their intermediate affinity for water.
  • Why is understanding protein folding important for comprehending protein structure and function in biological systems?
    Understanding protein folding is crucial because the specific three-dimensional structure a protein adopts determines its function in biological systems. Misfolding can lead to loss of function or diseases, so knowing how proteins fold helps explain their roles and mechanisms in the body.
  • What is the main non-covalent interaction that drives protein folding, and how does it affect the positioning of amino acids?
    The hydrophobic effect is the main driving force, causing non-polar amino acids to cluster inside the protein and polar or charged amino acids to be on the surface.
  • How does Leventhal's paradox demonstrate that protein folding is not a random process?
    Leventhal's paradox shows that if folding were random, it would take longer than the age of the universe, but proteins fold in less than a second, indicating a predictable, non-random pathway.
  • Where are non-polar, polar, and charged amino acids typically found in a folded protein, and why?
    Non-polar amino acids are found in the interior, charged amino acids on the surface, and polar amino acids can be found both inside and outside due to their intermediate affinity for water.
  • What role do cooperative stepwise interactions play in protein folding?
    Cooperative stepwise interactions between amino acids speed up folding by providing shortcuts, allowing proteins to reach their native structure quickly.
  • Why is understanding protein folding important for studying protein function in biological systems?
    Understanding folding is crucial because a protein's three-dimensional structure determines its function, and misfolding can lead to loss of function or disease.
  • What mnemonic can help you remember the non-polar amino acids, and why are these amino acids found in the protein's interior?
    The mnemonic 'GAV LIMP way fast' helps remember non-polar amino acids, which are found in the interior because they are hydrophobic and avoid water.