Objectively judging the quality of a protein structure from a Ramachandran plot

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Objectively judging the quality of a protein structure from a Ramachandran plot

MOTIVATION Statistical methods that compare observed and expected distributions of experimental observables provide powerful tools for the quality control of protein structures. The distribution of backbone dihedral angles ('Ramachandran plot') has often been used for such quality control, but without a firm statistical foundation. RESULTS A new and-simple method is presented for judging the ...

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Comment on "Revisiting the Ramachandran plot from a new angle".

that the ‘‘forbidden [bridge] region is well-populated in folded proteins, which can provide longer-range intramolecular hydrogen-bond partners.’’ However, using only a hard sphere model, Ramachandran and colleagues predicted the f and c combinations as a function of s that are observed in proteins of known structure. In particular, they showed that f and c combinations in the bridge region are...

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Revisiting the Ramachandran plot from a new angle.

The pioneering work of Ramachandran and colleagues emphasized the dominance of steric constraints in specifying the structure of polypeptides. The ubiquitous Ramachandran plot of backbone dihedral angles (ϕ and ψ) defined the allowed regions of conformational space. These predictions were subsequently confirmed in proteins of known structure. Ramachandran and colleagues also investigated the in...

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Ramachandran plot on the web

A graphics package has been developed to display the main chain torsion angles phi, psi (phi, Psi); (Ramachandran angles) in a protein of known structure. In addition, the package calculates the Ramachandran angles at the central residue in the stretch of three amino acids having specified the flanking residue types. The package displays the Ramachandran angles along with a detailed analysis ou...

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ژورنال

عنوان ژورنال: Bioinformatics

سال: 1997

ISSN: 1367-4803,1460-2059

DOI: 10.1093/bioinformatics/13.4.425