Ramachandran plot on the web

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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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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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Redrawing the Ramachandran plot after inclusion of hydrogen-bonding constraints.

A protein backbone has two degrees of conformational freedom per residue, described by its ϕ,ψ-angles. Accordingly, the energy landscape of a blocked peptide unit can be mapped in two dimensions, as shown by Ramachandran, Sasisekharan, and Ramakrishnan almost half a century ago. With atoms approximated as hard spheres, the eponymous Ramachandran plot demonstrated that steric clashes alone elimi...

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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 based on an intensity estimate with a two-dimensional Sobolev kernel

A Computational complexity As discussed in the Experiments, we used the high-dimensional synthetic data to consider our method’s computational complexity. The effect of the dimensionality d was negligible in practice, because the main calculations rely only on an n⇥ n Gram matrix whose calculation is relatively fast even for high dimensions. Our method’s time complexity scales as O(n2) as shown...

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ژورنال

عنوان ژورنال: Bioinformatics

سال: 2002

ISSN: 1367-4803,1460-2059

DOI: 10.1093/bioinformatics/18.11.1548