<p>The residues (labeled) of the SH2 domain that form hydrogen bonds with at least one of the 12 peptidomimetics are shown. The top figure shows a cartoon representation of the SH2 domain and the bottom figure shows a surface representation. The surface coloring shows the Coulombic electrostatic potential in different regions of the surface of the SH2 domain. The potential ranges from positive (in blue) to negative (in red). Note that a hydrogen bond is ignored if it is present in less than 50% of the conformations in the 10 ns molecular dynamics trajectory.</p
<p>The images depict membrane interaction areas of the WT (A) and H1047R mutant (B) first cluster re...
<p>The surface of the protein is colored based on the electrostatic potential. NAMN (orange) and res...
The difference in the frequency of pair residue hydrogen bonds for macro-states M0–M3 compared to ma...
<p>The bent binding mode of peptidomimetic comp70 (in green) is shown. The peptidomimetic is in comp...
<p>Hydrogen bond occupancy plots for each peptidomimetic are shown. In each sub-plot, the x-axis rep...
<p>The proposed novel wedged binding mode of peptidomimetic comp121 (in green) is shown. The peptido...
<p>Docked conformation of each peptidomimetic that was obtained using our incremental docking protoc...
<p>(a) RMSD plots for Shh backbone during 2 ns MD simulations for following complex structures: Shh-...
<p>(A) The average number of hydrogen bonds over the MD simulation between water and, in blue, the p...
<p>The H-bonds are highlighted in red. The different colors indicate the different locations of the ...
<p>Residues involved in hydrogen bonding during the last 6.0 ns of each simulation.</p
<p>Front view and back view of surface electrostatic potential map for the snapshots shown in <a hre...
<p>(A) Substrate binding cleft of hNtaq1. Carbon in the substrate-mimicking peptide, catalytic triad...
<p>The black lines represent hydrogen bonds; residues in green are in the <i>strand</i> state. Hydro...
<p>(A) A hydrogen bond network stabilizes the position of Arg37, pointing to the central axis of the...
<p>The images depict membrane interaction areas of the WT (A) and H1047R mutant (B) first cluster re...
<p>The surface of the protein is colored based on the electrostatic potential. NAMN (orange) and res...
The difference in the frequency of pair residue hydrogen bonds for macro-states M0–M3 compared to ma...
<p>The bent binding mode of peptidomimetic comp70 (in green) is shown. The peptidomimetic is in comp...
<p>Hydrogen bond occupancy plots for each peptidomimetic are shown. In each sub-plot, the x-axis rep...
<p>The proposed novel wedged binding mode of peptidomimetic comp121 (in green) is shown. The peptido...
<p>Docked conformation of each peptidomimetic that was obtained using our incremental docking protoc...
<p>(a) RMSD plots for Shh backbone during 2 ns MD simulations for following complex structures: Shh-...
<p>(A) The average number of hydrogen bonds over the MD simulation between water and, in blue, the p...
<p>The H-bonds are highlighted in red. The different colors indicate the different locations of the ...
<p>Residues involved in hydrogen bonding during the last 6.0 ns of each simulation.</p
<p>Front view and back view of surface electrostatic potential map for the snapshots shown in <a hre...
<p>(A) Substrate binding cleft of hNtaq1. Carbon in the substrate-mimicking peptide, catalytic triad...
<p>The black lines represent hydrogen bonds; residues in green are in the <i>strand</i> state. Hydro...
<p>(A) A hydrogen bond network stabilizes the position of Arg37, pointing to the central axis of the...
<p>The images depict membrane interaction areas of the WT (A) and H1047R mutant (B) first cluster re...
<p>The surface of the protein is colored based on the electrostatic potential. NAMN (orange) and res...
The difference in the frequency of pair residue hydrogen bonds for macro-states M0–M3 compared to ma...