<p>(A) Model reconstructions of PgdS in solution. Right: <i>ab initio</i> models from DAMMIF model; left, superposition of DAMMIF and CORAL model. The missing loops are represented as dummy residues colored cyan. Two orientations are shown. The domain 1, 2 and 3 are colored in green, blue and yellow, respectively. The relative positions of the N/C terminal and the functional catalytic core are also labeled. (B) Superimposed of two models of PgdS in a compact state (pH 5.0) and in an extended state (pH 8.0). The domain 2 and domain 3 are colored in grey, whereas domain 1 are colored in yellow (compact state) or blue (extended state).</p
A, R.m.s.d. of the models over time. The traces are color-coded: dark cyan, PRN-GLH-C; light lime, P...
<p>Superposition of initial structures of Cldn15 used in the monomer and the single-pore (Model1) an...
<p>The additional glycine residues are represented by the CPK model. The N, A, B, B′ and C-domains o...
<p>The α-helices and β-strands of three domains are colored with different colors (upper). The catal...
<p><b>A</b>. and <b>B</b>. Schematic cartoon representations of the pseudo-atomic solution structure...
<p>(a) Alignment of PMF-G with a representative TFP (1IQ9), color coded by residue type (acidic, red...
<p><b>Copyright information:</b></p><p>Taken from "Can molecular dynamics simulations help in discri...
<p>(A) Superimposition of the docking poses of PPT, PPD and TCDD (green, blue, and dark-gray sticks,...
<p>(A–E) Bound Gd ions and the interacting residues are depicted as yellow spheres and licorice mode...
<p>(A) The backbone atoms (N, C<sup>α</sup>, C′) for the best 15 models as superimposed by MOLMOL<i>...
<p>(A) Models of Kgp and RgpB based on the coordinates from PDB (1cvr.pdb), highlighting the cystein...
<p>A: MD runs APO1 (red) and APO2 (firebrick). B: MD runs ADP1 (blue) and ADP2 (light blue). C: MD r...
<p>Models of gp120 molecules from (A) CH40, (B) CH77, and (C) CH58 are shown as white surface projec...
Fifteen monomers form each one of the structures, and in both cases one monomer is colored in orange...
<p>Panel (A) represents the average fluctuations of Cα atoms represented by B-factors per residue ca...
A, R.m.s.d. of the models over time. The traces are color-coded: dark cyan, PRN-GLH-C; light lime, P...
<p>Superposition of initial structures of Cldn15 used in the monomer and the single-pore (Model1) an...
<p>The additional glycine residues are represented by the CPK model. The N, A, B, B′ and C-domains o...
<p>The α-helices and β-strands of three domains are colored with different colors (upper). The catal...
<p><b>A</b>. and <b>B</b>. Schematic cartoon representations of the pseudo-atomic solution structure...
<p>(a) Alignment of PMF-G with a representative TFP (1IQ9), color coded by residue type (acidic, red...
<p><b>Copyright information:</b></p><p>Taken from "Can molecular dynamics simulations help in discri...
<p>(A) Superimposition of the docking poses of PPT, PPD and TCDD (green, blue, and dark-gray sticks,...
<p>(A–E) Bound Gd ions and the interacting residues are depicted as yellow spheres and licorice mode...
<p>(A) The backbone atoms (N, C<sup>α</sup>, C′) for the best 15 models as superimposed by MOLMOL<i>...
<p>(A) Models of Kgp and RgpB based on the coordinates from PDB (1cvr.pdb), highlighting the cystein...
<p>A: MD runs APO1 (red) and APO2 (firebrick). B: MD runs ADP1 (blue) and ADP2 (light blue). C: MD r...
<p>Models of gp120 molecules from (A) CH40, (B) CH77, and (C) CH58 are shown as white surface projec...
Fifteen monomers form each one of the structures, and in both cases one monomer is colored in orange...
<p>Panel (A) represents the average fluctuations of Cα atoms represented by B-factors per residue ca...
A, R.m.s.d. of the models over time. The traces are color-coded: dark cyan, PRN-GLH-C; light lime, P...
<p>Superposition of initial structures of Cldn15 used in the monomer and the single-pore (Model1) an...
<p>The additional glycine residues are represented by the CPK model. The N, A, B, B′ and C-domains o...