This document discusses Ramachandran plots, which are used to visualize protein backbone structures and calculate possible phi and psi bond angles in amino acid residues. Ramachandran plots show favored, allowed, and generously allowed regions for different bond angles based on analysis of crystal structure data and distributions of over 9,000 amino acid residues. Two high-density areas correspond to alpha-helices and beta-structures. Glycine and proline residues have fewer allowed regions due to their side chain properties.