Activity 4/5.2 What Predictions Can You Make about the Behavior of Organic Macromolecules If You Know Their Structure? 1. Twenty amino acids are commonly utilized in the synthesis of proteins. These amino acids differ in the chemical properties of their side chains (also called R groups). What properties does each of the following R groups have? (Note: A side chain may display more than one of these properties.) R Group acidic or Polar or nonpolar? Hydrophilic or neutral? hydrophobic? a. Neutral Nonpolar Hydrophobic b. Acidic Polar Hydrophilic c. Basic Polar Hydrophilic d. Neutral Hydrophilic 2. Polypeptides and proteins are made up of linear sequences of amino acids. In its functional form, each protein has a specific three-dimensional structure or shape. Interactions among the individual amino acids and their side chains play a major role in determining this shape. a. How are amino acids linked together to form polypeptides or proteins? What is this type of bond called? Amino acids are covalently linked together via peptide bonds to form polypeptides or proteins. (See Figure 5.18, in 7th edition.) Biology, b. Define the four structures of a protein. c. What kinds of bonds hold each of these together? Primary: Covalent peptide bonds formed by The linear sequence of amino acids in a dehydration reactions hold the individual polypeptide or protein amino acids together in the polypeptide chain. Secondary: The secondary structure results from H helix or pleated sheet conformations bonding relationships set up between the H occurring at regular intervals along the attached to the N in one amino acid and the O polypeptide attached to the C of another amino acid. (See Figure 5.20.) Tertiary: Hydrogen and covalent bonds between side The folded or functional conformation chains (R groups) of various amino acids of a protein contribute, as do hydrophobic interactions and van der Waals interactions.
Activity 4/5.2 What Predictions Can You Make about the Behavior of Organic Macromolecules If You Know Their Structure? 1. Twenty amino acids are commonly utilized in the synthesis of proteins. These amino acids differ in the chemical properties of their side chains (also called R groups). What properties does each of the following R groups have? (Note: A side chain may display more than one of these properties.) R Group acidic or neutral? Polar or nonpolar? Hydrophilic or hydrophobic? a. Neutral Nonpolar Hydrophobic b. Acidic Polar Hydrophilic c. Basic Polar Hydrophilic d. Neutral Hydrophilic 2. Polypeptides and proteins are made up of linear sequences of amino acids. In its functional form, each protein has a specific three-dimensional structure or shape. Interactions among the individual amino acids and their side chains play a major role in determining this shape. a. How are amino acids linked together to form polypeptides or proteins? What is this type of bond called? Amino acids are covalently linked together via peptide bonds to form polypeptides or proteins. (See Figure 5.18, in Biology, 7th edition.) b. Define the four structures of a protein. c. What kinds of bonds hold each of these together? Primary: The linear sequence of amino acids in a polypeptide or protein Covalent peptide bonds formed by dehydration reactions hold the individual amino acids together in the polypeptide chain. Secondary: helix or pleated sheet conformations occurring at regular intervals along the polypeptide The secondary structure results from H bonding relationships set up between the H attached to the N in one amino acid and the O attached to the C of another amino acid. (See Figure 5.20.) Tertiary: The folded or functional conformation of a protein Hydrogen and covalent bonds between side chains (R groups) of various amino acids contribute, as do hydrophobic interactions and van der Waals interactions.
answer%20key%20to%20prediction%20macromolecule%20ws.docx