1 / 15

The relative orientation observed for  helices packed on ß sheets

The relative orientation observed for  helices packed on ß sheets. The Complementary twist model for the  helix to ß sheet packing. 6. 7. 2. 3. 1. 5. 4. 3. 4. 1. 2. Beta sheet structure. Beta sheets have “topologies” that bring together distant portions of the sequence.

glora
Download Presentation

The relative orientation observed for  helices packed on ß sheets

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. The relative orientation observed for  helices packed on ß sheets

  2. The Complementary twist model for the  helix to ß sheet packing

  3. 6 7 2 3 1 5 4 3 4 1 2 Beta sheet structure • Beta sheets have “topologies” that bring together distant portions of the sequence. Front: 1-2-5 Back: 7-6-3-4 Beta strands are numbered in sequence order. 2-1-4-3

  4. The relative orientation of the packing ß sheet

  5. Parallel beta sheetsConcanavalin

  6. ß-pleated sheet sandwich proteins

  7. A model for the aligned packing of the ß sheet

  8. The ß sheet to ß sheet packing in prealbumin

  9. Orthogonal Beta Sheet Protein

  10. A model for the orthogonal packing of the ß sheet

  11. B-propeller from flu virus

  12. B-barrel Porin (Channel) Protein

  13. What accounts for the high stability of HD-Crys? Hydrophobic domain cores Domain interface interactions

  14. N-terminal Met43 Phe56 Ile81 C-terminal Leu145 Val132 Val170 Hydrophobic domain interface residues N-terminal domain C-terminal domain Conservation among 35 -crystallin sequences:

  15. N-terminal Gln54 Arg79 C-terminal Gln143 Met147 Peripheral domain interface residues N-terminal domain C-terminal domain Conservation among 35 -crystallin sequences:

More Related