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5. Imagine a fully folded protein in tertiary structure. It looks like the image to the right where it
is lots of beta-strands with one alpha helix interacting on those beta-strands. The interaction
between the beta-strands and the alpha helix are held there by van der Waals interactions
forming a hydrophobic core between the two types of secondary structure in the cytoplasm.
Circle the amino acids that are involved in that interaction. WENQWKQELDTRYRNALQ 6. In
the sequence below, circle those residues that would not be involved in the hydrophobic core and
would rather interact with water. WENQWKQELDTRYRNALQ 7. The polypeptide below
forms a beta-hairpin, consisting of two antiparallel betastrands connected by a beta-turn. You
have found that the amide nitrogen of phenylalanine forms a hydrogen bond with the carbonyl
oxygen of threonine. Mark the peptide sequence below to indicate which residues belong to the
two beta-strands and which to the beta-turn. Explain your reasoning.

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5- Imagine a fully folded protein in tertiary structure- It looks like.docx

  • 1. 5. Imagine a fully folded protein in tertiary structure. It looks like the image to the right where it is lots of beta-strands with one alpha helix interacting on those beta-strands. The interaction between the beta-strands and the alpha helix are held there by van der Waals interactions forming a hydrophobic core between the two types of secondary structure in the cytoplasm. Circle the amino acids that are involved in that interaction. WENQWKQELDTRYRNALQ 6. In the sequence below, circle those residues that would not be involved in the hydrophobic core and would rather interact with water. WENQWKQELDTRYRNALQ 7. The polypeptide below forms a beta-hairpin, consisting of two antiparallel betastrands connected by a beta-turn. You have found that the amide nitrogen of phenylalanine forms a hydrogen bond with the carbonyl oxygen of threonine. Mark the peptide sequence below to indicate which residues belong to the two beta-strands and which to the beta-turn. Explain your reasoning.