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Tertiary Structures

Tertiary Structures. Cf myoglobin, RNAse, cytochrome C, and lysozyme Mb – high %age of -helix Cytochrome C –less -helix, some -sheet. RNAse – more -sheet Lysozyme – both in good measure. Figure 6-18. 6-18 b. 6-18c. Interior of protein.

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Tertiary Structures

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  1. Tertiary Structures • Cf myoglobin, RNAse, cytochrome C, and lysozyme • Mb – high %age of -helix • Cytochrome C –less -helix, some -sheet. • RNAse – more -sheet • Lysozyme – both in good measure

  2. Figure 6-18

  3. 6-18 b

  4. 6-18c

  5. Interior of protein • Interior contains mostly hydrophobic residues which stabilize structure, • But small proteins need more bonds • Disulfide • Other prosthetic groups (heme, e.g.) covalently attached

  6. Table 6-2

  7. Supersecondary structures (motifs or folds) • Combinations which recur • Organization of structures (SCOP)

  8. Folding regularities (not exhaustive) • -- loop • - corner

  9. 6-20a

  10. 6-20a (right)

  11. Folding regularities (cont) • -helices and -sheets usually are found in different layers (they don’t readily H-bond to each other)

  12. Folding regularities (cont) • Polypeptide chains adjacent in primary structure usually adjacent in tertiary structure

  13. Folding regularities (cont) • No crosses or knots

  14. 6-20b (left)

  15. 6-20b (right)

  16. Folding regularities (cont) • The  conformation most stable with a right hand twist •  sheets have a crossover strand, which usually is a “right handed connection” • Twisting larger scale structures result

  17. 6-20d

  18. 6-21a

  19. 6-22

  20. 6-22

  21. 6-22

  22. 6-22

  23. SCOP • Class • Fold • Family- significant primary sequence similarity and/or similar structure and function (globins, e.g.) • Superfamily – significant structural and funcional similarity (little primary structure similarity)

  24. Quaternary Structure • Multimers • Dimers • Oligomers • Protomers

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