Dihedral Angles of Biological Molecules
The backbone dihedral angles of proteins are called φ (phi, involving the backbone atoms C'-N-Cα-C'), ψ (psi, involving the backbone atoms N-Cα-C'-N) and ω (omega, involving the backbone atoms Cα-C'-N-Cα). Thus, φ controls the C'-C' distance, ψ controls the N-N distance and ω controls the Cα-Cα distance.
The planarity of the peptide bond usually restricts to be 180° (the typical trans case) or 0° (the rare cis case). The distance between the Cα atoms in the trans and cis isomers is approximately 3.8 and 2.9 Å, respectively. The cis isomer is mainly observed in Xaa-Pro peptide bonds (where Xaa is any amino acid).
The sidechain dihedral angles of proteins are denoted as χ1-χ5, depending on the distance up the sidechain. The χ1 dihedral angle is defined by atoms N-Cα-Cβ-Cγ, the χ2 dihedral angle is defined by atoms Cα-Cβ-Cγ-Cδ, and so on.
The sidechain dihedral angles tend to cluster near 180°, 60°, and −60°, which are called the trans, gauche+, and gauche- conformations. The choice of sidechain dihedral angles is affected by the neighbouring backbone and sidechain dihedrals; for example, the gauche+ conformation is rarely followed by the gauche+ conformation (and vice versa) because of the increased likelihood of atomic collisions.
Dihedral angles have also been defined by the IUPAC for other molecules, such as the nucleic acids (DNA and RNA) and for polysaccharides.
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