User:Karsten Theis/turns
From Proteopedia
(Difference between revisions)
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===Exercise 3=== | ===Exercise 3=== | ||
| - | Compare and contrast the two turns we discussed, and compare them to alpha helix and beta sheet. Clicking the buttons will preserve the orientation of the 2->3 peptide plane while adjusting the torsion angles. You can press the last button to flip the entire molecules as a rigid body (different from the pepflip button above, which changes torsion angles). | + | Compare and contrast the two turns we discussed, and compare them to alpha helix and beta sheet. Clicking the buttons will preserve the orientation of the 2->3 peptide plane <jmol> |
| + | <jmolLink> | ||
| + | <script> | ||
| + | define current selected; | ||
| + | select 68.CA or 68.C or 69.N or 69.H or 69.CA; | ||
| + | selectionHalos on; | ||
| + | delay 0.5; | ||
| + | selectionHalos off; | ||
| + | select current; | ||
| + | </script> | ||
| + | <text>☼</text> | ||
| + | </jmolLink> | ||
| + | </jmol> while adjusting the torsion angles. You can press the last button to flip the entire molecules as a rigid body (different from the pepflip button above, which changes torsion angles). | ||
<jmol> | <jmol> | ||
Revision as of 21:31, 7 February 2025
A beta turn is a secondary structure element consisting of four consecutive amino acids (or three peptide planes). The geometry of turns correspond to a change in the direction of the polypeptide backbone, allowing them to connect alpha helices and beta strands at the surface of a globular protein. Of the six main chain hydrogen bonding partners of a turn, a maximum of two are engaged in hydrogen bonding, and turns are rarely found in the hydrophobic core.
Exploring turns
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