User:Karsten Theis/turns
From Proteopedia
(Difference between revisions)
| Line 174: | Line 174: | ||
select 68.C or 68.O or 69.N or 69.H; | select 68.C or 68.O or 69.N or 69.H; | ||
spacefill off; | spacefill off; | ||
| - | select selected and | ||
select current; | select current; | ||
</script> | </script> | ||
| - | <text>☼</text> | + | <text>(☼)</text> |
</jmolLink> | </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> 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). | ||
Revision as of 21:35, 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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