(A) PLP RMSD values based on four 1 μs simulations of WT, E266K, R267H, and P300L. The blue plot represents WT, whereas E266K is shown in yellow, R267H is shown in purple, and P300L is shown in green. (B) RMSD distribution of PLP in each variant and WT. WT shows a much narrower distribution than the 3 variants. The color scheme is the same as in panel A. The representative PLP snapshots in the pocket are shown by (C) WT, (D) E226K, (E) R26H, and (F) P300L. The opposite monomer is colored in purple, and the amino acid substitutions are shown in green.</p
<p>(A) Control plots representing the stability of the models during the molecular dynamics run. The...
a) RMSD analysis was carried out for the molecular dynamics simulations of each system considering b...
<p>A) Representative conformations from 20ns molecular dynamics runs for M128V and HRdup PrP. α-heli...
A) Starting structure of the hGOT1 monomer showing PLP bound (colored in cyan) in the pocket (the mo...
(A) Key residues involved in PLP stabilization in the hGOT1 binding site based on the PDB ID 3II0. (...
(A) Location of amino acids subject to mutation relative to the ligand (S43) binding site (based on ...
<p>Comparison of wt and 116G PrP via MD simulations. (<b>a</b>) Cartoon representation of wild type ...
(A) Closed and (B) open states of hGOT1 produced by 1 μs MD simulation. The cofactor is represented ...
<p><b>(A)</b> The root mean square deviations (RMSDs) from the initial coordinates computed on the C...
<p>A) The evolution of the RMSD (Root Mean Square Deviation) of WT-g14-3-3 (in red) and Pho-g14-3-3 ...
Left: Location of amino acids subject to mutation relative to the ligand (GRL-0617) binding site (ba...
<p>A) Representation of the N-terminal binding pockets of HLA-B*2705 presenting pVIPR in non-canonic...
A) Visualization of PC1 positive displacement (shown by yellow arrows) from PCA. Negative displaceme...
<p>Panel A shows the change in the RMSD of the WT MPP structure over the course of a 100 ns simulati...
<p>a. MD simulation trajectory for unbound HtrA2. b. RMSF graph for GQYYFV bound HtrA2. c. RMSF grap...
<p>(A) Control plots representing the stability of the models during the molecular dynamics run. The...
a) RMSD analysis was carried out for the molecular dynamics simulations of each system considering b...
<p>A) Representative conformations from 20ns molecular dynamics runs for M128V and HRdup PrP. α-heli...
A) Starting structure of the hGOT1 monomer showing PLP bound (colored in cyan) in the pocket (the mo...
(A) Key residues involved in PLP stabilization in the hGOT1 binding site based on the PDB ID 3II0. (...
(A) Location of amino acids subject to mutation relative to the ligand (S43) binding site (based on ...
<p>Comparison of wt and 116G PrP via MD simulations. (<b>a</b>) Cartoon representation of wild type ...
(A) Closed and (B) open states of hGOT1 produced by 1 μs MD simulation. The cofactor is represented ...
<p><b>(A)</b> The root mean square deviations (RMSDs) from the initial coordinates computed on the C...
<p>A) The evolution of the RMSD (Root Mean Square Deviation) of WT-g14-3-3 (in red) and Pho-g14-3-3 ...
Left: Location of amino acids subject to mutation relative to the ligand (GRL-0617) binding site (ba...
<p>A) Representation of the N-terminal binding pockets of HLA-B*2705 presenting pVIPR in non-canonic...
A) Visualization of PC1 positive displacement (shown by yellow arrows) from PCA. Negative displaceme...
<p>Panel A shows the change in the RMSD of the WT MPP structure over the course of a 100 ns simulati...
<p>a. MD simulation trajectory for unbound HtrA2. b. RMSF graph for GQYYFV bound HtrA2. c. RMSF grap...
<p>(A) Control plots representing the stability of the models during the molecular dynamics run. The...
a) RMSD analysis was carried out for the molecular dynamics simulations of each system considering b...
<p>A) Representative conformations from 20ns molecular dynamics runs for M128V and HRdup PrP. α-heli...