Ramachandran plot
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, is a way to visualize energetically allowed regions for backbone dihedral angles ψ against φ of amino a…
What is Ramachandran plot in biology?
Ramachandran Plot : Polypeptide chain conformation. Ramachandran plot is a plot of the torsional angles – phi (φ)and psi (ψ) – of the residues (amino acids) contained in a peptide.
What do the colors in a Ramachandran plot mean?
(B) Diagram of a typical Ramachandran plot (φ/ψ plot). The regions marked “Core” correspond to conformations that do not have any steric hindrance. The yellow areas labeled “Allowed” correspond to conformations that could be possible if the atoms could come a little closer together.
What do the allowed regions of the Ramachandran plot show?
In theory, the allowed regions of the Ramachandran plot show which values of the Phi/Psi angles are possible for an amino acid, X, in a ala-X-ala tripeptide (Ramachandran et al., 1963). In practice, the distribution of the Phi/Psi values observed in a protein structure can be used for structure validation (Ramakrishnan et al., 2007).
How do side chains affect the Ramachandran plot?
Either case is usually shown against outlines for the theoretically favored regions. One might expect that larger side chains would result in more restrictions and consequently a smaller allowable region in the Ramachandran plot, but the effect of side chains is small.
What is the principle of Ramachandran diagram?
The Ramachandran Principle says that alpha helices, beta strands, and turns are the most likely conformations for a polypeptide chain to adopt, because most other conformations are impossible due to steric collisions between atoms.
What is Ramachandran plot biology discussion?
Plots of phi versus psi dihedral angles for amino acid residues are called Ramachandran plots. One can tell if the backbone is following a helical or an extended beta strand structure based on the values of the phi-psi angles over a length of backbone (usually 3-4 residues is sufficient).
What are the application of Ramachandran plot?
A Ramachandran plot can be used in two somewhat different ways. One is to show in theory which values, or conformations, of the ψ and φ angles are possible for an amino-acid residue in a protein (as at top right).
Which is the first quadrant in Ramachandran plot?
The Ramachandran Plot helps with determination of secondary structures of proteins. Quadrant I shows a region where some conformations are allowed. This is where rare left-handed alpha helices lie.
When was the Ramachandran plot first calculated?
The first Ramachandran plot was calculated just after the first protein structure at atomic resolution was determined ( myoglobin, in 1960 ), although the conclusions were based on small-molecule crystallography of short peptides.
What is the angle of a Ramachandran plot?
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, is a way to visualize energetically allowed regions for backbone dihedral angles ψ against φ ...
How to read Ramachandran plot?
How to read Ramachandran plot? A Ramachandran plot is a way to visualize backbone dihedral angles ψ against φ of amino acid residues in protein structure. A Ramachandran plot can be used in two somewhat different ways. One is to show in theory which values, or conformations, of the ψ and φ angles, are possible for an amino-acid residue in a protein. A second is to show the empirical distribution of data points observed in a single structure .
Who is G N Ramachandran?
Gopalasamudram Narayana Ramachandran (8 October 1922 – 7 April 2001) is an Indian biophysicist and crystallographer who, along with Gopinath Kartha, worked out the triple helical structure of collagen. G N Ramachandran is an Indian biophysicist who was known for his work that led to his creation of the Ramachandran plot for understanding peptide ...
When was the torsional angle plot developed?
The plot was developed in 1963 by G. N. Ramachandran, by plotting the φ values on the x-axis and the ψ values on the y-axis, as for the image at left. Plotting the torsional angles in this way graphically shows which combination of angles is possible. What Is Peptide Linkage?
What are functionally relevant residues?
Functionally relevant residues. Functionally relevant residues may occasionally have torsion angles that plot to the disallowed regions of a Ramachandran plot. The specific geometry of these functionally relevant residues, while energetically unfavorable, may be important for the protein’s function, catalytic or otherwise.
Most recent answer
Ramachandran plot for protein is a map of allowed and disallowed conformation ( https://en.wikipedia.org/wiki/Conformational_isomerism) of region of protein.
All Answers (30)
Ramachandran plot is when on x-axis You put value of phi torsion angle, and on y-axis psi angle is. Both from one residue of protein. By comparing position of your residue on that plot, with a model plot where allowed and favourite areas are marked You can evaluate structure of Your protein.
Overview
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, 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 definitio…
Uses
A Ramachandran plot can be used in two somewhat different ways. One is to show in theory which values, or conformations, of the ψ and φ angles are possible for an amino-acid residue in a protein (as at top right). A second is to show the empirical distribution of datapoints observed in a single structure (as at right, here) in usage for structure validation, or else in a database of many structures (as in the lower 3 plots at left). Either case is usually shown against outlines for the th…
Amino-acid preferences
One might expect that larger side chains would result in more restrictions and consequently a smaller allowable region in the Ramachandran plot, but the effect of side chains is small. In practice, the major effect seen is that of the presence or absence of the methylene group at Cβ. Glycine has only a hydrogen atom for its side chain, with a much smaller van der Waals radius than the CH3, CH2, or CH group that starts the side chain of all other amino acids. Hence it is least re…
More recent updates
The first Ramachandran plot was calculated just after the first protein structure at atomic resolution was determined (myoglobin, in 1960 ), although the conclusions were based on small-molecule crystallography of short peptides. Now, many decades later, there are tens of thousands of high-resolution protein structures determined by X-ray crystallography and deposited in the Protein Data Bank (PDB). Many studies have taken advantage of this data to produce more detai…
Related conventions
One can also plot the dihedral angles in polysaccharides (e.g. with CARP).
Gallery
• Ramachandran plot for the general case; data from Lovell 2003
• Ramachandran plot for Glycine
• Ramachandran plot for Proline
• Ramachandran plot for pre-Proline
Software
• Web-based Structural Analysis tool for any uploaded PDB file, producing Ramachandran plots, computing dihedral angles and extracting sequence from PDB
• Web-based tool showing Ramachandran plot of any PDB entry
• MolProbity web service that produces Ramachandran plots and other validation of any PDB-format file
Further reading
• 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., available on-line at Anatax
• Branden, C.-I.; Tooze, J. (1991), Introduction to Protein Structure, Garland Publishing, NY, ISBN 0-8153-0344-0
Who Is G N Ramachandran?
Ramachandran Plot and Peptide Torsion Angles
Secondary Structure Plot Regions
Plot Regions Limited by Steric Hindrance
Ramachandran Plot Explanation
- (Smart Notes Description) How to read Ramachandran plot? A Ramachandran plot is a way to visualize backbone dihedral angles ψ against φ of amino acid residues in protein structure. A Ramachandran plot can be used in two somewhat different ways. One is to show in theory which values, or conformations, of the ψ and φ angles, are possible for an amino...
Final Words