1 / 24

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.

langer
Download Presentation

Tertiary Structures

An Image/Link below is provided (as is) to download presentation Download Policy: Content on the Website is provided to you AS IS for your information and personal use and may not be sold / licensed / shared on other websites without getting consent from its author. Content is provided to you AS IS for your information and personal use only. Download presentation by click this link. While downloading, if for some reason you are not able to download a presentation, the publisher may have deleted the file from their server. During download, if you can't get a presentation, the file might be deleted by the publisher.

E N D

Presentation Transcript

  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

More Related