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Understanding the Orientation and Stability of Alpha Helices and Beta Sheets in Protein Structures

This document explores the relative orientation of alpha helices packed on beta sheets, detailing the complementary twist model that describes their interaction. It discusses beta sheet topology, strand numbering, and structures such as parallel beta sheets and their packing in proteins like prealbumin and flu virus B-barrels. The focus is on the stability provided by hydrophobic domain cores and interface interactions among residues of various domains, including conservation patterns observed across 35 gamma-crystallin sequences.

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Understanding the Orientation and Stability of Alpha Helices and Beta Sheets in Protein Structures

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  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:

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