Hemoglobin dihedral symmetry

There are several forms of rotational symmetry. The simplest is cyclic symmetry, involving rotation about a single axis (Fig. 4—24a). If subunits can be superimposed by rotation about a single axis, the protein has a symmetry defined by convention as Gn (C for cyclic, n for the number of subunits related by the axis). The axis itself is described as an w-fold rotational axis. The a/3 protomers of hemoglobin (Fig. 4-23) are related by C2 symmetry. A somewhat more complicated rotational symmetry is dihedral symmetry, in which a twofold rotational axis intersects an w-fold axis at right angles. The symmetry is defined as DTO (Fig. 4—24b). A protein with dihedral symmetry has 2n protomers. 

If the a and /3 chains are considered to be identical, then hemoglobin has dihedral symmetry with two rotational axes, and with the four subunits arranged at the apices of the tetrahedron. 

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