Ramachandran Plot in Biology

The Ramachandran plot depicts the statistical distribution of the backbone dihedral angle combinations and. In theory, the Ramachandran plot’s permissible regions illustrate which Phi/Psi angles are possible for an amino acid, X, in an ala-Xla tripeptide (Ramachandran et al., 1963). The Ramachandran plot depicts energetically permissible and forbidden dihedral angle areas. Many dihedral angles are discovered in the banned zones of the Ramachandran plot for poor quality homology models. Such variances usually suggest a structural issue.

Ramachandran Plot

• The Ramachandran plot can be used to assess the precision of a protein structure prediction. Ramachandran plots are generated using a variety of programmes and servers, The structural stereochemical property is predicted by the Ramachandran plot. The PROCHECK examines the overall model geometry as well as the geometry of each individual residue to determine the stereochemical quality of a predicted model. Model validation, which can be done using Ramachandran plot analysis, comes after protein structure prediction, refinement, and model quality assessment. Servers require a file format for protein structures and utilise quantum mechanics to calculate the fraction of favoured, allowed, and banned regions. The phi and psi angles of the backbone, the energy of hydrogen bonds, peptide bond planarity, and steric conflicts all go into the calculation

• Global checks on the model’s geometry, stereochemistry, and other structural features can provide the next indication of its overall quality. Such tests are easily accessible on the internet. The Ramachandran plot of the protein’s − main-chain torsion angles is the best of these, as it may quickly detect proteins with an excessive number of outlying residues. Ramachandran plots for current protein structures are available on several websites

• Through the hard-sphere model describing steric coupling effects, the Ramachandran map covering the phi and psi angles is a fundamental theoretical feature for estimating the allowable conformational space of an amino acid in a polypeptide. 37 Without the involvement of phi and psi angles, the structure of the protein is significantly constrained by steric hindrances. The shape of a structure that has been experimentally identified is mapped onto phi–psi space and observed. The two-dimensional map discriminates the phi and psi space into the allowed and prohibited region by outlining the inhabited sections if the Ramachandran plot is created with a well-resolved protein structure database

Principle of Ramachandran diagram

Because most alternative conformations are unattainable due to steric collisions between atoms, the Ramachandran Principle states that alpha helices, beta strands, and turns are the most likely conformations for a polypeptide chain to adopt.

The torsional angles are graphically plotted in this fashion to indicate which angles can be combined. By situating its planar peptide bond relative to the two neighbouring planar peptide bonds, the torsional angles of each residue in a peptide dictate the geometry of its attachment to its two adjacent residues, and therefore the torsional angles govern the conformation of the residues and the peptide. Because of steric hindrance, many angle combinations and, as a result, residue conformations are not conceivable. Protein structural scientists can use a Ramachandran plot to establish which torsional angles are allowed and get information into the structure of peptides. The Ramachandran plot of ribonuclease His shown on the right.

Applications of Ramachandran plot

There are two alternative ways to use a Ramachandran plot. One is to show in principle which values of and angles are possible for an amino-acid residue in a protein. The second is to display the empirical distribution of data points observed in a single structure (as seen at the right) used for structure validation, or in a database of multiple structures (as in the lower 3 plots at left). In either scenario, outlines for the supposedly favoured locations are frequently shown.

Conclusion

The Ramachandran plot is a fundamental concept in structural biology that can be found in both publications and textbooks. We are still learning more about the basic principles of protein structure as the number of known protein structures grows and the accuracy of ultra-high resolution protein structures improves. We study novel approaches to express some of the essential elements of the Ramachandran plot and of protein conformation using high fidelity conformational information, such as geo-style and wrapped Ramachandran plots. We emphasise the urgent need for a standardised nomenclature for peptide conformation and suggest one.