<p>Backbone RMSF per residue reported for n-HRP (black) and p-HRP (red) along the analyzed time frames. The gray bands indicate the helix and sheet regions of HRP according to the crystallographic structure.</p
<p>(A) RMSD<sub>Cα</sub> of sampled conformations during five cMD simulations with different atomic ...
<p>Left: GluK2-<i>trans</i> complex; right: GluK2-<i>cis</i> complex. Data obtained from five indepe...
<p>Secondary structure elements limits are indicated by horizontal bars on the upper x axis. Regions...
<p>(A) Backbone RMSD with respect to the starting structure during the entire course of 100 ns MD si...
<p>The RMSD was calculated over the whole simulation process to check the stability of the unmodifie...
<p>Structural stability of the HIF-2α protein backbone compared between the simulated systems. For c...
<p>Equilibrium simulations were performed using AhR<sub>HIF</sub> and AhR<sub>CLOCK</sub> models emp...
<p>(A) Plot of the Backbone RMSD of TAZ2 along the simulation. The MD was fitted against the average...
The RMSF analysis of all-atom simulations exhibit similar atomic flexibilities of AWSEM- and AlphaFo...
<p>(A) Backbone RMSD (Å) relative to the crystal structure for the average structure obtained from t...
<p>For each graph, an experimental measure (grey) is compared to the flexibility calculated from a s...
<p>The solid lines indicate the mean values of groupM (red) and groupL (blue). The dotted lines are ...
<p>(A) RMSFs as calculated from MD simulations for MHC and peptide residues (inset). Only positions ...
<p>(A) The backbone atom root mean square deviation (RMSD) for apo, inhibitor bound, apo (truncated)...
<p>RMSF was measured from a trajectory pooled from the final 400 ns of each replicate simulation, fo...
<p>(A) RMSD<sub>Cα</sub> of sampled conformations during five cMD simulations with different atomic ...
<p>Left: GluK2-<i>trans</i> complex; right: GluK2-<i>cis</i> complex. Data obtained from five indepe...
<p>Secondary structure elements limits are indicated by horizontal bars on the upper x axis. Regions...
<p>(A) Backbone RMSD with respect to the starting structure during the entire course of 100 ns MD si...
<p>The RMSD was calculated over the whole simulation process to check the stability of the unmodifie...
<p>Structural stability of the HIF-2α protein backbone compared between the simulated systems. For c...
<p>Equilibrium simulations were performed using AhR<sub>HIF</sub> and AhR<sub>CLOCK</sub> models emp...
<p>(A) Plot of the Backbone RMSD of TAZ2 along the simulation. The MD was fitted against the average...
The RMSF analysis of all-atom simulations exhibit similar atomic flexibilities of AWSEM- and AlphaFo...
<p>(A) Backbone RMSD (Å) relative to the crystal structure for the average structure obtained from t...
<p>For each graph, an experimental measure (grey) is compared to the flexibility calculated from a s...
<p>The solid lines indicate the mean values of groupM (red) and groupL (blue). The dotted lines are ...
<p>(A) RMSFs as calculated from MD simulations for MHC and peptide residues (inset). Only positions ...
<p>(A) The backbone atom root mean square deviation (RMSD) for apo, inhibitor bound, apo (truncated)...
<p>RMSF was measured from a trajectory pooled from the final 400 ns of each replicate simulation, fo...
<p>(A) RMSD<sub>Cα</sub> of sampled conformations during five cMD simulations with different atomic ...
<p>Left: GluK2-<i>trans</i> complex; right: GluK2-<i>cis</i> complex. Data obtained from five indepe...
<p>Secondary structure elements limits are indicated by horizontal bars on the upper x axis. Regions...
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