Outline
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Introduction (Figure 6.1)
Secondary Structure: Regular Ways to Fold the Polypeptide Chain
Discovery of Regular Polypeptide Structures (Figure 5.12b, Figure 6.2, Figure 6.3, Figure 6.4)
Describing the Structures: Molecular Helices and Pleated Sheets (Figure 6.5, Figure 6.6, Table 6.1)
Ramachandran Plots (Figure 6.2, Figure 6.8, Figure 6.9, Figure 6.10)
Fibrous Proteins: Structural Materials of Cells and Tissues (Table 6.2)
The Keratins (Figure 6.11)
Fibroin (Figure 6.12, Table 6.2)
Collagen
Collagen Structure (Figure 6.13, Figure p. 179)
Collagen Synthesis (Figure 6.14)Elastin (Unnumbered Figure)
Globular Proteins: Tertiary Structure and Functional Diversity
Different Folding for Different Functions (Figure 6.1, Figure 6.16)
Varieties of Globular Protein Structure: Patterns of Folding (Figure 6.16, Figure 6.17, Figure 6.18, Figure 6.19)
Factors Determining Secondary and Tertiary Structure
The Information for Protein Folding (Figure 6.20)
The Thermodynamics of Folding
Conformational Entropy
Charge-Charge Interactions
Internal Hydrogen Bonds (Figure 6.21)
van der Waals Interactions (Table 6.3)
The Hydrophobic Effect (Table 6.4, Figure 6.22)The Role of Disulfide Bonds (Figure 6.23)
Dynamics of Globular Protein Structure
Kinetics of Protein Folding (Figure 6.24)
Kinetics of Disulfide Bond Formation (Figure 6.25)
Chaperonins (Figure 6.26)
Motions Within Globular Protein Molecules (Table 6.5)
Prions - Protein Folding and Mad Cow Disease (Figure 6.27)
Prediction of Secondary and Tertiary Protein Structure
Prediction of Secondary Structure (Table 6.6, Figure 6.28)
Tertiary Structure: Computer Simulation of Folding
Quaternary Structure of Proteins (Figure 6.29)
Multisubunit Proteins: Homotypic Protein-Protein Interactions (Figure 6.30, Figure 6.32, Figure 6.33)
Heterotypic Protein-Protein Interactions