Organic Chemistry and Polymers (cont’d). Copyright © Houghton Mifflin Company. All rights reserved. 22d–2 Amino Acids di-functional group compounds, carboxylic.

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Presentation transcript:

Organic Chemistry and Polymers (cont’d)

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

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

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

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)

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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