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Ramachandran plot
Visual representation of allowable protein conformations / From Wikipedia, the free encyclopedia
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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. The figure on the left illustrates the definition of the φ and ψ backbone dihedral angles[2] (called φ and φ' by Ramachandran). The ω angle at the peptide bond is normally 180°, since the partial-double-bond character keeps the peptide bond planar.[3] The figure in the top right shows the allowed φ,ψ backbone conformational regions from the Ramachandran et al. 1963 and 1968 hard-sphere calculations: full radius in solid outline, reduced radius in dashed, and relaxed tau (N-Cα-C) angle in dotted lines.[4] Because dihedral angle values are circular and 0° is the same as 360°, the edges of the Ramachandran plot "wrap" right-to-left and bottom-to-top. For instance, the small strip of allowed values along the lower-left edge of the plot are a continuation of the large, extended-chain region at upper left.
![Thumb image](http://upload.wikimedia.org/wikipedia/commons/thumb/4/43/1axc_PCNA_ProCheck_Rama.jpg/320px-1axc_PCNA_ProCheck_Rama.jpg)
![Thumb image](http://upload.wikimedia.org/wikipedia/commons/thumb/8/85/Ramachandran_plot_original_outlines.jpg/320px-Ramachandran_plot_original_outlines.jpg)
![Thumb image](http://upload.wikimedia.org/wikipedia/commons/thumb/9/97/Protein_backbone_PhiPsiOmega_drawing.svg/320px-Protein_backbone_PhiPsiOmega_drawing.svg.png)