User:Karsten Theis/turns

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<jmol>
<jmol>
<jmolButton>
<jmolButton>
-
<script>rphi2 = 60 - angle({67.C},{68.N},{68.CA},{68.C});rotate branch {68.CA} {68.N} @rphi2;rpsi2 = 30 - angle({68.N},{68.CA},{68.C},{69.N});rotate branch {68.C} {68.CA}@rpsi2;rphi3 = 90 - angle({68.C},{69.N},{69.CA},{69.C});rotate branch {69.N} {69.CA} @rphi3;rpsi3 = 0 - angle({69.N},{69.CA},{69.C},{70.N});rotate branch {69.CA} {69.C} @rpsi3;center visible</script>
+
<script>rphi2 = 60 - angle({67.C},{68.N},{68.CA},{68.C});rotate branch {68.CA} {68.N} @rphi2;rpsi2 = 30 - angle({68.N},{68.CA},{68.C},{69.N});rotate branch {68.C} {68.CA}@rpsi2;rphi3 = 90 - angle({68.C},{69.N},{69.CA},{69.C});rotate branch {69.N} {69.CA} @rphi3;rpsi3 = 0 - angle({69.N},{69.CA},{69.C},{70.N});rotate branch {69.CA} {69.C} @rpsi3</script>
<text>Type I prime</text>
<text>Type I prime</text>
</jmolButton>
</jmolButton>

Revision as of 20:50, 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

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

Karsten Theis

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