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In biochemistry, a Ramachandran plot (also known as a Rama plot, a Ramachandran diagram or a [φ,ψ] plot), originally developed in 1963 by G. N. Ramachandran, C. Ramakrishnan, and V. Sasisekharan, [1] is a way to visualize energetically allowed regions for backbone dihedral angles ψ against φ of amino acid residues in protein structure.
A special way for plotting and visualization of protein torsion angles was introduced by Ramachandran and co-authors and has since then been called the Ramachandran plot. In the Ramachandran plot, we can view the distribution of torsion angles in a protein structure (image below).
Ramachandran plot is the plot of angles called psi (ψ) and phi (φ) of the residues (commonly known as amino acids) present in a peptide. It assess the stereochemical quality of protein structures by plotting the phi (ϕ) and psi (ψ) dihedral angles of amino acid residues.
The Ramachandran plot is a powerful tool for analyzing protein conformation, folding, and stability. Its utilization aids in deciphering protein structure, predicting structures, and refining protein models.
A Ramachandran plot, also known as a Ramachandran diagram or a φ-ψ plot, is a way to visualize energetically allowed regions for backbone dihedral angles ψ (psi) against φ (phi) of amino acid residues in protein structures.
Ramachandran Plot. In subject area: Biochemistry, Genetics and Molecular Biology. Ramachandran plot is a two-dimensional (2D) plot of the torsional angles of amino acids φ (phi) and ψ (psi) in a protein sequence. From: Molecular Docking for Computer-Aided Drug Design, 2021. Add to Mendeley.
A Ramachandran plot, also known as a Ramachandran diagram or a [φ,ψ] plot, was originally developed by Gopalasamudram Ramachandran, an Indian physicist, in 1963. Ramachandran Plot is a way to visualize dihedral angles ψ against φ of amino acid residues in protein structure.
The present web utility provides a very convenient way to plot all types of Ramachandran maps, 2D & 3D plots, six distinct categories of maps:, Gly, Val/Ile, pre-Pro, trans-Pro, cis-Pro & Ala (plus remaining 15 amino acids) (Chen et al., 2010).
The Ramachandran plot is a plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in a peptide. In sequence order, φ is the C (i-1),N (i),Ca (i),C (i) torsion angle and ψ is the N (i),Ca (i),C (i),N (i+1) torsion angle.
The Ramachandran plot maps the allowed regions of phi and psi dihedral angles in protein backbone structures. It revealed that phi and psi angles are restricted to specific regions to avoid steric clashes between atoms. The main allowed regions correspond to alpha-helical and beta-sheet conformations.