1. Organic Chemistry and Polymers (cont’d)

2. Copyright © Houghton Mifflin Company. All rights reserved. 22d–2 Amino Acids di-functional group compounds, carboxylic acid and amine functinal groups  -aminocarboxylic acid - meaning that the amine functional group is one carbon removed from the carboxylic acid functional group

3. Copyright © Houghton Mifflin Company. All rights reserved. 22d–3 p.591b

4. Copyright © Houghton Mifflin Company. All rights reserved. 22d–4 Common Amino Acids

5. Copyright © Houghton Mifflin Company. All rights reserved. 22d–5 Figure 22.18: The 20 α-amino acids found in most proteins. [ Nonpolar R Groups ] (cont’d)

6. Copyright © Houghton Mifflin Company. All rights reserved. 22d–6 Figure 22.18: The 20 α-amino acids found in most proteins. [ Polar R Groups ]

7. Copyright © Houghton Mifflin Company. All rights reserved. 22d–7 Figure 22.18: The 20 α-amino acids found in most proteins. [ Polar R Groups ]

8. Copyright © Houghton Mifflin Company. All rights reserved. 22d–8 Figure 22.18: The 20 α-amino acids found in most proteins. [ Nonpolar R Groups ]

9. Copyright © Houghton Mifflin Company. All rights reserved. 22d–9 Figure 22.18: The 20 α-amino acids found in most proteins. [ Polar R Groups ]

10. Copyright © Houghton Mifflin Company. All rights reserved. 22d–10 Figure 22.28: Tetrahedral carbon atom has four different substituents

11. Copyright © Houghton Mifflin Company. All rights reserved. 22d–11 Tertiary Structure of Proteins overall three-dimensional structure of the protein

12. Copyright © Houghton Mifflin Company. All rights reserved. 22d–12 p.593

13. Copyright © Houghton Mifflin Company. All rights reserved. 22d–13 Tripeptide containing glycine, cysteine, and alanine Source: Photo Researchers, Inc.

14. Copyright © Houghton Mifflin Company. All rights reserved. 22d–14 Figure 22.19: The amino acid sequences in (a) oxytocin and (b) vasopressin

15. Copyright © Houghton Mifflin Company. All rights reserved. 22d–15 Figure 22.20: Hydrogen bonding within a protein chain

16. Copyright © Houghton Mifflin Company. All rights reserved. 22d–16 Figure 22.21: Ball-and-stick model of a portion of a protein chain

17. Copyright © Houghton Mifflin Company. All rights reserved. 22d–17 Figure 22.22: Hydrogen bonding

18. Copyright © Houghton Mifflin Company. All rights reserved. 22d–18 Figure 22.23: (a) collagen (b) pleated sheet arrangement of many proteins bound together to from the elongated protein found in silk fibers

19. Copyright © Houghton Mifflin Company. All rights reserved. 22d–19 Secondary Structure of Protein Regular patterns in the structure created by intramolecular hydrogen bonding

20. Copyright © Houghton Mifflin Company. All rights reserved. 22d–20 Figure 22.24: Protein myoglobin

21. Copyright © Houghton Mifflin Company. All rights reserved. 22d–21 Figure 22.25: Summary of the various types of interactions that stabilize the tertiary structure of protein

22. Copyright © Houghton Mifflin Company. All rights reserved. 22d–22 Figure 22.26: Permanent waving of hair

23. Copyright © Houghton Mifflin Company. All rights reserved. 22d–23 Figure 22.27: Schematic representation of the thermal denaturation of a protein