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A dihedral angle is the angle between two intersecting planes or half-planes. ... This is the case for kinematic chains or amino acids in a protein structure. In ...
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, [1] is a way to visualize energetically allowed regions for backbone dihedral angles ( also called as torsional angles , phi and psi angles ) ψ ...
Thus, the γ-turn has two forms, a classical form with (φ, ψ) dihedral angles of roughly (75°, −65°) and an inverse form with dihedral angles (−75°, 65°). At least eight forms of the beta turn occur, varying in whether a cis isomer of a peptide bond is involved and on the dihedral angles of the central two residues.
In biochemistry, a Janin plot, like a Ramachandran plot, is a way to visualize dihedral angle distributions in protein structures. While a Ramachandran plot relates the two backbone dihedral angles, a Janin plot relates the first side chain dihedral angle χ-1 against χ-2.
In more general terms, they adopt dihedral angles such that the ψ dihedral angle of one residue and the φ dihedral angle of the next residue sum to roughly −105°. As a consequence, α-helical dihedral angles, in general, fall on a diagonal stripe on the Ramachandran diagram (of slope −1), ranging from (−90°, −15°) to (−70°, − ...
Backbone-dependent rotamer library for serine.Each plot shows the population of the χ 1 rotamers of serine as a function of the backbone dihedral angles φ and ψ. In biochemistry, a backbone-dependent rotamer library provides the frequencies, mean dihedral angles, and standard deviations of the discrete conformations (known as rotamers) of the amino acid side chains in proteins as a function ...
The first approach uses discrete variables for representing the coordinates or the dihedral angles of the protein structure. The variables are originally all continuous values and, to transform them into discrete values, a discretization process is typically applied. The second approach uses continuous variables for the coordinates or dihedral ...
However, this still leaves the phi-psi angles of the backbone, and up to four dihedral angles for each side chain, leading to a worst case complexity of k 6*n possible states of the protein, where n is the number of residues and k is the number of discrete states modeled for each dihedral angle. In order to reduce the conformational space, one ...