<p>The H-bonds are highlighted in red. The different colors indicate the different locations of the amino acids within the protein. Blue and green represent interior amino acids. The amino acids on the surface of the protein are shown in ball representation. Orange represents the superficial amino acids that were highly contacted by solvent. These images were drawn using Swiss-PdbViewer.</p
<p>The amino acids with negative charge, positive charge, polar and hydrophobic side chains are show...
(A) Snapshot of the initial unbound configuration. The protein (brown) and DNA (light blue) are show...
The composition of protein surfaces determines both affinity and specificity of protein-protein inte...
<p>(A) Hydrogen bonding profile indicating numbers of hydrogen bonds formed within protein atoms and...
<p>Left. Closeup of the YtvA chromophore (in green) with the amino acids considered in this study re...
<p>The surface of the protein is colored based on the electrostatic potential. NAMN (orange) and res...
Abstract—Protein is the major component of the organism. It has a unique three-dimensional structure...
<p>FhCL3 residues interacting with Nitrile (A), HTS12701 (B), BTB03219 (C). Ligands (violet) and pro...
<p>The mapped amino acids are shown as red spheres, and residues Ser70, Lys73 and Glu166 as green sp...
<p>The middle square boxes represent the specific amino acid. The background color of the box gives ...
<p>(<b>A–D</b>) Each panel is composed of three snapshots. On the left is the APoc superimposition o...
<p>Rendering of the three hexamer structures showing top and bottom views, with both electrostatic p...
<p>The protein is shown as cartoon, overlaid with its semi-transparent surface representation. Amino...
<p>The residues (labeled) of the SH2 domain that form hydrogen bonds with at least one of the 12 pep...
<p>The ribbons with different colors represent the four parts constituting the preproinsulin molecul...
<p>The amino acids with negative charge, positive charge, polar and hydrophobic side chains are show...
(A) Snapshot of the initial unbound configuration. The protein (brown) and DNA (light blue) are show...
The composition of protein surfaces determines both affinity and specificity of protein-protein inte...
<p>(A) Hydrogen bonding profile indicating numbers of hydrogen bonds formed within protein atoms and...
<p>Left. Closeup of the YtvA chromophore (in green) with the amino acids considered in this study re...
<p>The surface of the protein is colored based on the electrostatic potential. NAMN (orange) and res...
Abstract—Protein is the major component of the organism. It has a unique three-dimensional structure...
<p>FhCL3 residues interacting with Nitrile (A), HTS12701 (B), BTB03219 (C). Ligands (violet) and pro...
<p>The mapped amino acids are shown as red spheres, and residues Ser70, Lys73 and Glu166 as green sp...
<p>The middle square boxes represent the specific amino acid. The background color of the box gives ...
<p>(<b>A–D</b>) Each panel is composed of three snapshots. On the left is the APoc superimposition o...
<p>Rendering of the three hexamer structures showing top and bottom views, with both electrostatic p...
<p>The protein is shown as cartoon, overlaid with its semi-transparent surface representation. Amino...
<p>The residues (labeled) of the SH2 domain that form hydrogen bonds with at least one of the 12 pep...
<p>The ribbons with different colors represent the four parts constituting the preproinsulin molecul...
<p>The amino acids with negative charge, positive charge, polar and hydrophobic side chains are show...
(A) Snapshot of the initial unbound configuration. The protein (brown) and DNA (light blue) are show...
The composition of protein surfaces determines both affinity and specificity of protein-protein inte...