True/False Statements: Please determine if the statements are true or false. 1. Disulfide bonding between amino acid side chains within the same protein sub-unit is considered secondary structure, while disulfide bonding between amino acid side chains of two different protein sub-units is considered quaternary structure. 2. Hydrogen bonding between two amino acid side chains within the same protein sub-unit contributes to tertiary structure, while hydrogen bonding between two amino acid side chains of two different protein sub-units contributes to quaternary structure. 3. A supersecondary structure is a compact three-dimensional protein structure of several adjacent elements of a secondary structure that is smaller than a protein domain or a subunit. Supersecondary structures can act as nucleations (or initiating points) in the process of protein folding. 4. The hydrophobic effect has the greatest influence on protein stability and is a major determinant of native protein structure; it leads to the polar side chains of amino acid residues minimizing their contact with water. Multiple Choice Questions: Please choose the most appropriate answer and fill this out on your scantron form. Only one answer is correct for each problem. 5. Protein denaturation can occur if each of the following applications are used. Please choose the best combination of matching Roman numerals (I,II,III, IV) representing terms and numbers (ā ā”ā¢ā£) representing the description. I. Heating II. pH variations III. Detergents IV. Chaotropic reagents ā Associate with nonpolar residues, interfering with hydrophobic interactions essential for native structure ā” Alter ionization states of aa residue side chains, changing charge distributions, and H-bonding ⢠Ions or small organic molecules like urea that increase solubility of nonpolar substances in water ⣠Affects conformation. Entire polypeptide unfolds or melts (A) ā matches with I. ā” matches with II. ⢠matches with III. ⣠matches with IV. (B) ā matches with IV. ā” matches with III. ⢠matches with II. ⣠matches with I. (C) ā matches with II. ā” matches with III. ⢠matches with IV. ⣠matches with I. (D) ā matches with IV. ā” matches with I. ⢠matches with III. ⣠matches with II. (E) ā matches with III. ā” matches with II. ⢠matches with IV. ⣠matches with I. 6. For the peptide N-Met-Gly-Pro-Glu-Arg-Asn-Ala-Ala-Pro-Ala-Gly-Pro-Gln-C. there are statements listed below. I. This peptide contains 13 amino acids in 11 peptide bonds. II. This peptide contains 13 amino acids in 12 peptide bonds. III. This peptide contains 13 amino acids in 13 peptide bonds. IV. This sequence would form an excellent α helix. V. This sequence would not form an excellent α helix. VI. At a neutral pH, the charge of this peptide is 0 VII. At a neutral pH, the charge of this peptide is -1 The true statements above include: (A) I, V, VI (B) II, IV, VI (C) II, V, VI (D) III, IV, VII (E) III, V, VII