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Ramachandran plot

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For more information, log on to-http://shomusbiology.weebly.com/Download the study materials here-http://shomusbiology.weebly.com/bio-materials.htmlThis video explains the importance of Ramachandran plot to study protein chemistry.A Ramachandran plot (also known as 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 backbone dihedral angles ψ against φ of amino acid residues in protein structure. The figure at 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 planar.[3] The figure at 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-Calpha-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 Source of the article published in description is Wikipedia. I am sharing their material. © by original content developers of Wikipedia.Link- http://en.wikipedia.org/wiki/Main_Page Biochemistry, 4th EditionDonald Voet, Judith G. VoetNovember 2010, ©2011

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