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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?
In an α-helix, which amino acids are considered strong helix formers?
In an α-helix, which amino acids are considered strong helix formers?
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?
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?
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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?
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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?
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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?
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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?
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What creates a pleated sheet-like structure in a β sheet?
What creates a pleated sheet-like structure in a β sheet?
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In antiparallel β sheets, how are the H-bonded strands oriented?
In antiparallel β sheets, how are the H-bonded strands oriented?
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What type of interactions are called sheets in β structures?
What type of interactions are called sheets in β structures?
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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?
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Which factor contributes to peptide bonds being less reactive compared to esters?
Which factor contributes to peptide bonds being less reactive compared to esters?
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Why is rotation around the peptide bond not permitted?
Why is rotation around the peptide bond not permitted?
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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?
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What determines the secondary structure of a protein?
What determines the secondary structure of a protein?
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What is the energy change (ΔGº') for peptide bond hydrolysis?
What is the energy change (ΔGº') for peptide bond hydrolysis?
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What defines oligopeptides compared to polypeptides?
What defines oligopeptides compared to polypeptides?
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