. Nonpolar (hydrophobic) Nonpolar (hydrophobic) Amino Acid Side Chains

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. Nonpolar (hydrophobic) Nonpolar (hydrophobic) Amino Acid Side Chains Nonpolar (hydrophobic) Nonpolar (hydrophobic) . Nonpolar (hydrophobic) Polar Polar Polar FIGURE 22.1 The 20 amino acids that are the building blocks of proteins can be classified as (a ) nonpolar (hydrophobic), (b ) polar but neutral, (c ) acidic, or (d ) basic. Also shown here are the one-letter and three-letter codes used to denote amino acids. For each amino acid, the ball-and-stick (left) and space-filling (right) models show only the side chain. Acidic YOU MUST DEPROTENATE Acidic YOU MUST DEPROTENATE Figure 22-1 p595

Polar Polar Amino Acid Side Chains Nonpolar (hydrophobic) Nonpolar (hydrophobic) Polar Polar Polar Basic FIGURE 22.1 The 20 amino acids that are the building blocks of proteins can be classified as (a ) nonpolar (hydrophobic), (b ) polar but neutral, (c ) acidic, or (d ) basic. Also shown here are the one-letter and three-letter codes used to denote amino acids. For each amino acid, the ball-and-stick (left) and space-filling (right) models show only the side chain. Basic Basic Figure 22-1 p596

Primary Structure: Kinks and Planes

Secondary Structure: Alpha Helix Beta Sheet FIGURE 22.10 (a ) The α-helix. (b ) The β-pleated sheet structure. Figure 22-10 p611

Hydrogen Bonding in Beta Sheet

Tertiary Structure FIGURE 22.20 Forces that stabilize the tertiary structures of proteins. Note that the helical structure and the sheet structure are two kinds of backbone hydrogen bonding. Although the backbone hydrogen bonding is part of the secondary structure, the conformation of the backbone puts constraints on the possible arrangement of the side chains. Figure 22-20 p618

Quaternary Structure