The presence of these structures can be identified on hydrophilicity or hydrophobicity plots by a stretch of 20 positive values on the Kyte–Doolittle scale. A double minimum at 208 and 222 nanometers in circular dichroism spectroscopy is used to identify these structures. These structures have square-like cross sections that allow them to be differentiated from similar structures named for “310” and pi. Two of these structures are dimerized in the DNA-binding leucine zipper motif. (*) Glycine (-5[1])and proline are called “breakers” of these structures. (-5[1])A diagonal cluster on Ramachandran plots around dihedral angles of −60 (“negative 60”) and −45 (“negative 45”) degrees identifies (-5[1])these structures. (-5[1])Hydrogen bonds stabilize the 3.6 residues per turn (10[1])characteristic of these structures. For 10 points, name this coiled secondary (10[1])structure motif in proteins that is more common (10[1])than beta sheets. ■END■ (10[1]0[3])