Visual representation of allowable protein conformations
Original hard-sphere, reduced-radius, and relaxed-tau φ,ψ regions from Ramachandran, with updated labels and axesBackbone dihedral angles φ and ψ (and ω). All three angles are at 180° in the conformation shown
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.
A Ramachandran plot generated from human PCNA, a trimeric DNA clamp protein that contains both β-sheet and α-helix (PDB ID 1AXC). The red, brown, and yellow regions represent the favored, allowed, and "generously allowed" regions as defined by ProCheck
^Ramachandran, G.N.; Ramakrishnan, C.; Sasisekharan, V. (1963). "Stereochemistry of polypeptide chain configurations". Journal of Molecular Biology. 7: 95–9. doi:10.1016/S0022-2836(63)80023-6. PMID 13990617.
^Richardson, J.S. (1981). "The Anatomy and Taxonomy of Protein Structure". Anatomy and Taxonomy of Protein Structures. Advances in Protein Chemistry. Vol. 34. pp. 167–339. doi:10.1016/S0065-3233(08)60520-3. ISBN 9780120342341. PMID 7020376.
^Pauling, L.; Corey, H.R.; Branson, H. R. (1951). "The Structure of Proteins: Two Hydrogen-Bonded Helical Configurations of the Polypeptide Chain". Proceedings of the National Academy of Sciences of the United States of America. 37 (4): 205–211. Bibcode:1951PNAS...37..205P. doi:10.1073/pnas.37.4.205. PMC 1063337. PMID 14816373.
^Ramachandran, G.N.; Sasiskharan, V. (1968). Conformation of polypeptides and proteins. Advances in Protein Chemistry. Vol. 23. pp. 283–437. doi:10.1016/S0065-3233(08)60402-7. ISBN 9780120342235. PMID 4882249.
biochemistry, a Ramachandranplot (also known as a Rama plot, a Ramachandran diagram or a [φ,ψ] plot), originally developed in 1963 by G. N. Ramachandran, C. Ramakrishnan...
creating the Ramachandranplot K. V. Ramachandran (1898–1956), an Indian music and art critic M. Ramachandran, an Indian politician M. G. Ramachandran, also...
pattern of backbone dihedral angles in a particular region of the Ramachandranplot regardless of whether it has the correct hydrogen bonds. The concept...
x-axis). One of the dihedral angles in the backbones of proteins in a Ramachandranplot Internal or effective angle of friction. In cartography and navigation...
and 160 with an unknown role. Ramachandranplot Circuit topology Structural classification of proteins CATH HB plot Dot plot (bioinformatics) Self-similarity...
Eadie-Hofstee diagram Population pyramid Parametric plot Causality loop diagram Ramachandranplot V model Sentence diagram Tree structure Treemapping...
φ and ψ backbone dihedral angles of all residues and construct a Ramachandranplot. The side-chain of amino acids and the nature of interactions in the...
contains 182 residues, and is 67% helical. The mitochondrial ferritin's Ramachandranplot shows its structure to be mainly alpha helical with a low prevalence...
the field of chemistry. Ramachandranplot, Ramachandran map, and Ramachandran angles: The Ramachandranplot and Ramachandran map were developed by Gopalasamudram...
respectively). A Ramachandranplot (also known as a Ramachandran diagram or a [φ,ψ] plot), originally developed in 1963 by G. N. Ramachandran, C. Ramakrishnan...
Chennai Central (officially Puratchi Thalaivar Dr. M.G. Ramachandran Central Railway Station, formerly Madras Central)(station code: MAS), is an NSG–1...
near (φ, ψ) = (–135°, 135°) (broadly, the upper left region of the Ramachandranplot) diverge significantly from the fully extended conformation (φ, ψ)...
of the two amino acids that do not follow along with the typical Ramachandranplot, along with glycine. Due to the ring formation connected to the beta...
constrained to specific values of the dihedral angles ψ and φ on the Ramachandranplot. Both the α-helix and the β-sheet represent a way of saturating all...
a Janin plot, like a Ramachandranplot, is a way to visualize dihedral angle distributions in protein structures. While a Ramachandranplot relates the...
Kerala Particle physics 1961 Gopalasamudram Narayana Ramachandran Tamil Nadu Ramachandranplot 1962 Vikram Ambalal Sarabhai Gujarat Space science 1963...
side-chain orientation, analogous to the preferred backbone orientation of Ramachandranplots). It can potentially serve to elucidate protein folding as well as...
α-helical dihedral angles, in general, fall on a diagonal stripe on the Ramachandran diagram (of slope −1), ranging from (−90°, −15°) to (−70°, −35°). For...
helices can adopt backbone dihedral angles in some regions of the Ramachandranplot; thus, a segment of residues with such dihedral angles is often called...
and appearance that result from the lack of DNA repair enzymes. The Ramachandranplot shows that the secondary structure of the CRY1 protein is primarily...
overall CS23D score, knowledge-based score, chemical shift score, Ramachandranplot statistics, correlations between the observed and calculated shifts...
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