Podcast
Questions and Answers
Which type of amino acid is most likely to disrupt the α-helix structure due to impossible bond rotation?
Which type of amino acid is most likely to disrupt the α-helix structure due to impossible bond rotation?
- Leucine
- Alanine
- Proline (correct)
- Glycine
In an α-helix, which amino acids are considered strong helix formers?
In an α-helix, which amino acids are considered strong helix formers?
- Phenylalanine and Tryptophan
- Proline and Glycine
- Alanine and Leucine (correct)
- Lysine and Arginine
Which type of amino acid is known to have a positive charge on its side chain?
Which type of amino acid is known to have a positive charge on its side chain?
- Lysine (correct)
- Valine
- Serine
- Glutamine
How does the sequence of amino acids affect the stability of an α-helix?
How does the sequence of amino acids affect the stability of an α-helix?
Which feature of the peptide bond contributes to the large macroscopic dipole moment of the α-helix?
Which feature of the peptide bond contributes to the large macroscopic dipole moment of the α-helix?
Why are peptide bonds aligned roughly parallel with the helical axis in an α-helix?
Why are peptide bonds aligned roughly parallel with the helical axis in an α-helix?
What type of structure is formed by hydrogen bonds between the backbone amides in different strands of a β sheet?
What type of structure is formed by hydrogen bonds between the backbone amides in different strands of a β sheet?
Which type of β sheet has strands that are oriented in the same direction?
Which type of β sheet has strands that are oriented in the same direction?
What creates a pleated sheet-like structure in a β sheet?
What creates a pleated sheet-like structure in a β sheet?
In antiparallel β sheets, how are the H-bonded strands oriented?
In antiparallel β sheets, how are the H-bonded strands oriented?
What type of interactions are called sheets in β structures?
What type of interactions are called sheets in β structures?
How do the hydrogen bonds between strands in parallel β sheets differ from antiparallel β sheets?
How do the hydrogen bonds between strands in parallel β sheets differ from antiparallel β sheets?
Which factor contributes to peptide bonds being less reactive compared to esters?
Which factor contributes to peptide bonds being less reactive compared to esters?
Why is rotation around the peptide bond not permitted?
Why is rotation around the peptide bond not permitted?
In a fully extended polypeptide, what are the angles for rotation around the α carbon—amide nitrogen bond and the α carbon—carbonyl carbon bond?
In a fully extended polypeptide, what are the angles for rotation around the α carbon—amide nitrogen bond and the α carbon—carbonyl carbon bond?
What determines the secondary structure of a protein?
What determines the secondary structure of a protein?
What is the energy change (ΔGº') for peptide bond hydrolysis?
What is the energy change (ΔGº') for peptide bond hydrolysis?
What defines oligopeptides compared to polypeptides?
What defines oligopeptides compared to polypeptides?