Questions: Theoretically, a protein could assume a virtually infinite number of configurations and conformations. Which of the following features of proteins drastically limit the actual number of available conformations and configurations? (Select all that apply.) - Only L-amino acids (except for glycine) are used in proteins. - The tertiary structure of a protein is controlled by hydrophobic interactions between nonpolar amino acid residues. - Although any one of 20 amino acids is possible at each position, only one is used. - The Ramachandran angles φ and ψ are limited in their values due to steric restrictions. - The partial double bond character of the α-C-N bond in the peptide group limits the conformations of the peptide group.

Theoretically, a protein could assume a virtually infinite number of configurations and conformations. Which of the following features of proteins drastically limit the actual number of available conformations and configurations? (Select all that apply.) - Only L-amino acids (except for glycine) are used in proteins. - The tertiary structure of a protein is controlled by hydrophobic interactions between nonpolar amino acid residues. - Although any one of 20 amino acids is possible at each position, only one is used. - The Ramachandran angles φ and ψ are limited in their values due to steric restrictions. - The partial double bond character of the α-C-N bond in the peptide group limits the conformations of the peptide group.
Transcript text: Theoretically, a protein could assume a virtually infinite number of configurations and conformations. Which of the following features of proteins drastically limit the actual number of available conformations and configurations? (Select all that apply.) Only L-amino acids (except for glycine) are used in proteins. The tertiary structure of a protein is controlled by hydrophobic interactions between nonpolar amino acid residues. Although any one of 20 amino acids is possible at each position, only one is used. The Ramachandran angles $\varphi$ and $\psi$ are limited in their values due to steric restrictions. The partial double bond character of the $\alpha-\mathrm{C}-\mathrm{N}$ bond in the peptide group limits the conformations of the peptide group.
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Solution

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The answer includes the following options:

  1. Only L-amino acids (except for glycine) are used in proteins.
  2. The Ramachandran angles $\varphi$ and $\psi$ are limited in their values due to steric restrictions.
  3. The partial double bond character of the $\alpha-\mathrm{C}-\mathrm{N}$ bond in the peptide group limits the conformations of the peptide group.

Explanation for each option:

  1. Only L-amino acids (except for glycine) are used in proteins.

    • Correct. Proteins are composed almost exclusively of L-amino acids, which significantly reduces the number of possible configurations compared to if both L- and D-amino acids were used.

  2. The tertiary structure of a protein is controlled by hydrophobic interactions between nonpolar amino acid residues.

    • Incorrect. While hydrophobic interactions do influence the tertiary structure, they do not drastically limit the number of possible conformations and configurations in the same way as the other factors listed.

  3. Although any one of 20 amino acids is possible at each position, only one is used.

    • Incorrect. This statement is misleading. In reality, any of the 20 amino acids can be used at each position in a protein sequence, which does not limit the number of possible configurations.

  4. The Ramachandran angles $\varphi$ and $\psi$ are limited in their values due to steric restrictions.

    • Correct. The values of the Ramachandran angles $\varphi$ and $\psi$ are restricted due to steric hindrance, which limits the possible conformations of the protein backbone.

  5. The partial double bond character of the $\alpha-\mathrm{C}-\mathrm{N}$ bond in the peptide group limits the conformations of the peptide group.

    • Correct. The partial double bond character of the peptide bond restricts rotation around the $\alpha-\mathrm{C}-\mathrm{N}$ bond, thereby limiting the conformations that the peptide backbone can adopt.

Summary: The features of proteins that drastically limit the actual number of available conformations and configurations are:

  • Only L-amino acids (except for glycine) are used in proteins.
  • The Ramachandran angles $\varphi$ and $\psi$ are limited in their values due to steric restrictions.
  • The partial double bond character of the $\alpha-\mathrm{C}-\mathrm{N}$ bond in the peptide group limits the conformations of the peptide group.
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