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Tertiary Structures

Delve into the intricacies of tertiary protein structures, examining characteristics in myoglobin, RNAse, cytochrome C, and lysozyme. Discover key motifs, folding regularities, and the importance of supersecondary structures. Uncover insights on the stabilization and organization of protein interiors. Learn about quaternary structures and multimers, dimers, oligomers, and protomers.

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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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