<p>Left: Ramachandran plot for 1E0L of PSI libraries 3-20-mers. Middle: Superposition of the Ramachandran plot for 3-20-mers (blue) and 3-mers (purple). Right: Superposition of the Ramachandran plot for 3-20-mers (blue) and 3,6,9-mers (purple). Similar plots are obtained for all the other protein fragment libraries.</p
Three-dimensional protein structures usually contain regions of local order, called secondary struct...
<p>(a) Coordinate transformation applied to the Ramachandran plot in order to compute the Ramachandr...
<p>The different color codes indicate most favored (red), generously allowed (dark yellow), addition...
<p>(A) Ramachandran plot; (B) histogram of phi angles; (C) histogram of psi angles. Alpha-helix, bet...
A graphics package has been developed to display the main chain torsion angles phi, psi (phi, Psi); ...
<p>(a) The state of a residue within a peptide (top) and a peptoid (bottom) can be largely specified...
The red color region denotes residues of the protein in the most favored regions; the brown color de...
The Ramachandran plot displays the main chain conformation angles (\Phi and \Psi) of the polypeptide...
<p>Ramachandran plot showing the residues as square dots lying in the four different regions, most f...
BACKGROUND: The Ramachandran plot is a fundamental tool in the analysis of protein structures...
<p>(a) We construct by slicing across the Ramachandran plot, which can cause points distant in dihe...
The red color region denotes residues of the protein in the most favored regions; the brown color de...
<p>The polyproline II (1), extended beta (2) and right-handed alpha-helical (3) regions are marked. ...
<p>The Ramachandran plot shows phi-psi torsion angles of all residues in the structure. The coloring...
<p>Areas defined as red, yellow, light yellow and white indicate most favored, additional allowed, g...
Three-dimensional protein structures usually contain regions of local order, called secondary struct...
<p>(a) Coordinate transformation applied to the Ramachandran plot in order to compute the Ramachandr...
<p>The different color codes indicate most favored (red), generously allowed (dark yellow), addition...
<p>(A) Ramachandran plot; (B) histogram of phi angles; (C) histogram of psi angles. Alpha-helix, bet...
A graphics package has been developed to display the main chain torsion angles phi, psi (phi, Psi); ...
<p>(a) The state of a residue within a peptide (top) and a peptoid (bottom) can be largely specified...
The red color region denotes residues of the protein in the most favored regions; the brown color de...
The Ramachandran plot displays the main chain conformation angles (\Phi and \Psi) of the polypeptide...
<p>Ramachandran plot showing the residues as square dots lying in the four different regions, most f...
BACKGROUND: The Ramachandran plot is a fundamental tool in the analysis of protein structures...
<p>(a) We construct by slicing across the Ramachandran plot, which can cause points distant in dihe...
The red color region denotes residues of the protein in the most favored regions; the brown color de...
<p>The polyproline II (1), extended beta (2) and right-handed alpha-helical (3) regions are marked. ...
<p>The Ramachandran plot shows phi-psi torsion angles of all residues in the structure. The coloring...
<p>Areas defined as red, yellow, light yellow and white indicate most favored, additional allowed, g...
Three-dimensional protein structures usually contain regions of local order, called secondary struct...
<p>(a) Coordinate transformation applied to the Ramachandran plot in order to compute the Ramachandr...
<p>The different color codes indicate most favored (red), generously allowed (dark yellow), addition...