<p>(a) Alignment of PMF-G with a representative TFP (1IQ9), color coded by residue type (acidic, red; basic, blue; hydrophilic, purple; nonpolar, green; cysteine, yellow), with disulfide bonds denoted by the black lines; (b) secondary structure schematic comparing PMF-G (left) and a representative TFP (right; 1IQ9); (c) backbone model of PMF-G (20 lowest-energy conformers) with partially transparent surface rendering (both color coded N- to C-terminus, blue to red); (d) full surface rendering of PMF-G color coded by residue type (same color code as a); (e) surface rendering of 1IQ9 (same color code as a).</p
<p>a) Cartoon drawing of the lowest energy conformer of CTD. The two monomers are indicated by two d...
<p>The 3D-structure of dimer S-MB the open conformation was determined from the 10-nsec MD simulatio...
Surface representation of the density maps for a protomer of FMDV-AWH-W125 complex (A) and FMDV-AWH-...
<p>(a) Backbone model of PMF-G with the twenty lowest-energy conformers, color coded from N- to C-te...
<p>The green and red bars refer to the dimer and the monomer, respectively. The background is colour...
<p>A) Cartoon representation highlighting the cell binding sites P4 (magenta) and P8 (blue). B) Surf...
<p><b>A.</b> Contact probabilities of TF residues with MBP (top panel) and P2 (bottom panel). The ba...
<div><p>(A and B) Molecular surfaces of (A) PGRP-SA and (B) PGRP-LB shown in similar orientations. S...
<p>For subfigures a, b and c; the protein residues and ligands are in line and stick representations...
(a) The ribbon diagram shows the overall secondary structure of CCHFV-NP from strain YL04057 (PDB co...
<p>Only the protein backbone is shown in ribbon presentation. α-helices in blue, β-sheets in red, tu...
<p>Labels of 1 and 2 in the landscapes represent the initial (left) and the final (right) structures...
<p>Relative orientation of the functional surfaces in the model of active, nonphosphorylated (A) and...
<p>Homology models of four additional PMF isoforms that are highly expressed in <i>P. shermani</i> (...
<p>The residues with increased nonpolar surface exposed to the solvent are indicated in magenta, and...
<p>a) Cartoon drawing of the lowest energy conformer of CTD. The two monomers are indicated by two d...
<p>The 3D-structure of dimer S-MB the open conformation was determined from the 10-nsec MD simulatio...
Surface representation of the density maps for a protomer of FMDV-AWH-W125 complex (A) and FMDV-AWH-...
<p>(a) Backbone model of PMF-G with the twenty lowest-energy conformers, color coded from N- to C-te...
<p>The green and red bars refer to the dimer and the monomer, respectively. The background is colour...
<p>A) Cartoon representation highlighting the cell binding sites P4 (magenta) and P8 (blue). B) Surf...
<p><b>A.</b> Contact probabilities of TF residues with MBP (top panel) and P2 (bottom panel). The ba...
<div><p>(A and B) Molecular surfaces of (A) PGRP-SA and (B) PGRP-LB shown in similar orientations. S...
<p>For subfigures a, b and c; the protein residues and ligands are in line and stick representations...
(a) The ribbon diagram shows the overall secondary structure of CCHFV-NP from strain YL04057 (PDB co...
<p>Only the protein backbone is shown in ribbon presentation. α-helices in blue, β-sheets in red, tu...
<p>Labels of 1 and 2 in the landscapes represent the initial (left) and the final (right) structures...
<p>Relative orientation of the functional surfaces in the model of active, nonphosphorylated (A) and...
<p>Homology models of four additional PMF isoforms that are highly expressed in <i>P. shermani</i> (...
<p>The residues with increased nonpolar surface exposed to the solvent are indicated in magenta, and...
<p>a) Cartoon drawing of the lowest energy conformer of CTD. The two monomers are indicated by two d...
<p>The 3D-structure of dimer S-MB the open conformation was determined from the 10-nsec MD simulatio...
Surface representation of the density maps for a protomer of FMDV-AWH-W125 complex (A) and FMDV-AWH-...