<p>The secondary structure was generated using the STRIDE program implemented in VMD. Color scheme for secondary structure: purple for α-helix, yellow for extended β-strand, cyan for turn, and white for random. The N-terminus of each conformation was shown as a blue bead.</p
Extensive molecular dynamic simulations (similar to 240 ns) have been used to investigate the confor...
The conversion to a disease-associated conformer (PrP (Sc) ) of the cellular prion protein (PrP (C) ...
AbstractPrion proteins cause neurodegenerative illnesses in humans and animals. The diseases are ass...
<p>(A) The most populated β-hairpin structure for the WT, corresponding to the center of its third c...
<p>The N-terminal region and the C-terminal region are labeled by pink and green balls respectively....
<p>The calculated secondary structure probabilities for the WT PrP106-126 and its two mutants A117V,...
<p>Mutated residues are shown in red color, hydrophilic residues in blue and hydrophobic residues in...
<p>(<b>a</b>) Cluster analysis of the MD conformations picked every 10 ps over the 96 ns of producti...
<p>(A) Aligned structures for WT tau and (B) average backbone conformation for this cluster; (C) ali...
<p>Comparison of wt and 116G PrP via MD simulations. (<b>a</b>) Cartoon representation of wild type ...
Structural elements relevant for defining a more open or closed conformation are the regions of the ...
<p>(<b>A</b>) Superposed conformations were selected by RMSDs clustering. Ribbon diagrams display th...
<p>Protein backbone is rendered in ribbons, whereas Phe103, Ser181 and Thr274[Ala/Ile] side chains a...
<p>The subunit interface is rendered by van der Waals surface using the colors; green for chain A, b...
Extensive molecular dynamic simulations (similar to 240 ns) have been used to investigate the confor...
Extensive molecular dynamic simulations (similar to 240 ns) have been used to investigate the confor...
The conversion to a disease-associated conformer (PrP (Sc) ) of the cellular prion protein (PrP (C) ...
AbstractPrion proteins cause neurodegenerative illnesses in humans and animals. The diseases are ass...
<p>(A) The most populated β-hairpin structure for the WT, corresponding to the center of its third c...
<p>The N-terminal region and the C-terminal region are labeled by pink and green balls respectively....
<p>The calculated secondary structure probabilities for the WT PrP106-126 and its two mutants A117V,...
<p>Mutated residues are shown in red color, hydrophilic residues in blue and hydrophobic residues in...
<p>(<b>a</b>) Cluster analysis of the MD conformations picked every 10 ps over the 96 ns of producti...
<p>(A) Aligned structures for WT tau and (B) average backbone conformation for this cluster; (C) ali...
<p>Comparison of wt and 116G PrP via MD simulations. (<b>a</b>) Cartoon representation of wild type ...
Structural elements relevant for defining a more open or closed conformation are the regions of the ...
<p>(<b>A</b>) Superposed conformations were selected by RMSDs clustering. Ribbon diagrams display th...
<p>Protein backbone is rendered in ribbons, whereas Phe103, Ser181 and Thr274[Ala/Ile] side chains a...
<p>The subunit interface is rendered by van der Waals surface using the colors; green for chain A, b...
Extensive molecular dynamic simulations (similar to 240 ns) have been used to investigate the confor...
Extensive molecular dynamic simulations (similar to 240 ns) have been used to investigate the confor...
The conversion to a disease-associated conformer (PrP (Sc) ) of the cellular prion protein (PrP (C) ...
AbstractPrion proteins cause neurodegenerative illnesses in humans and animals. The diseases are ass...