The Ramachandran plots of glycine and pre-proline
- Abstract. The Ramachandran plot is a fundamental tool in the analysis of protein structures. ...
- Background. The Ramachandran plot [ 1] is the 2d plot of the φ-ψ torsion angles of the protein backbone. ...
- Results. ...
- Conclusion. ...
- Methods. ...
- Acknowledgements. ...
- Author information. ...
- Additional information. ...
- Authors’ original submitted files for images. ...
- Rights and permissions. ...
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 dots in the Ramachandran plot represent?
Each dot in the plot corresponds to an amino acid, with its φ and ψ angles. On the left is a structure at low resolution and on the right is a high-resolution structure. The Ramachandran plot shows the distribution of the torsion angles of a protein within certain regions.
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.
For what purpose Ramachandran diagram is used?
Ramachandran is used for the measurement of angles in amino acids (proteins), however, the principle can be adapted to measure angles in other types of molecules.
What is the role of Ramachandran plot in homology Modelling of proteins?
Ramachandran plot of a protein structure derived from homology modeling. It provides an overview of allowed and disallowed regions of torsion angle values, serving as an important indicator of the quality of protein three dimensional structures.
What are the principles underlying the formation of the Ramachandran plot?
Answer : 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.
How do you read a Ramachandran plot?
1:188:32How to Interpret Ramachandran Plots - YouTubeYouTubeStart of suggested clipEnd of suggested clipIs located at it's particular Phi and sy angle okay so you just you just plot the points okay andMoreIs located at it's particular Phi and sy angle okay so you just you just plot the points okay and every one of those dots represents an amino acid in a particular protein.
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?
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.
What is the Ramachandran plot?
The Ramachandran plot is among the most central concepts in structural biology , seen in publications and textbooks alike. However, with the increasing numbers of known protein-structures and greater accuracy of ultra-high resolution protein structures, we are still learning more about the basic principles of protein structure. Here we use high fidelity conformational information to explore novel ways, such a geo-style and wrapped Ramachandran plots, to convey some of the basic aspects of the Ramachandran plot and of protein conformation. We point out the pressing need for a standard nomenclature for peptide conformation and propose such a nomenclature. Finally, we summarize some recent conceptual advances related to the building blocks of protein structure. The results for linear groups imply the need for substantive revisions in how the basics of protein structure are handled.
When was Ramachandran plot developed?
Ramachandran plot also known as a Ramachandran diagram or [, ] plot was originally developed in 1963 by G. N. Ramachandran, C. Ramakrishnan and V. Sasisekharan. Ramachandran plot provides a simple two-dimensional graphic. representation of all possible protein structures in terms of torsion angles.
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