9. Look at the protein below. Label the diagram on the right and show which part of the protein has hydrophobic amino acid residues and what part of the protein has hydrophilic amino acid residues. Explain how you know.

1. Theoretically, a protein could assume a virtually infinite number of configurations and conformations. Suggestseveral features of proteins that drastically limit the actual number.    2. What are the greatest structural features that differentiate sphingolipids from phosphoglycerides?   3. High levels of glucose-6-phosphate inhibit glycolysis. If the concentration of glucose-6-phosphate decreases,activity is restored. Why?

5. Classify each of the following amino acids as polar or nonpolar and hydrophilic and hydrophobic. NH2 CH2 CH2 H2N-C-COOH H2N-C-COOH H. a. b. Polar or nonpolar: Hydrophilic or Hydrophobic:

On 4. Below is a polypeptide with an unknown number of amino acids. On the diagram below: a. Circle EVERY peptide bond b. Circle and number each amino acid from 1, 2, 3, and so on; from left to right c. Label each amino acid as polar, non-polar, or electrically charged d. Label the N-terminus and C-terminus e. Select three pairs of amino acids that could potentially interact to influence tertiary structure AND state the bond/force/interaction type involved in each pair. H₂N-CH-C-N-CH-C- CH₂ CH₂ CH₂ NH CINH NH₂ Accessibility: Investigate CH₂ -NH -CH-C-N- CH-OH CH3 -CH-C-N CH₂ CH₂ -N- OH CHIC-OH CH₂ OH