1. .
Nonpolar (hydrophobic)
Nonpolar (hydrophobic)
Amino Acid Side Chains
Nonpolar (hydrophobic)
Nonpolar (hydrophobic) .
Nonpolar (hydrophobic)
Polar
Polar
Polar
FIGURE 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

2. Polar
Polar
Amino Acid Side Chains
Nonpolar (hydrophobic)
Nonpolar (hydrophobic)
Polar
Polar
Polar
Basic
FIGURE 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

3. Primary Structure:
Kinks and Planes

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

5. Hydrogen Bonding in Beta Sheet

6. Tertiary Structure
FIGURE 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 p618

7. Quaternary Structure