<p>In the graphic, the β-sheet components turn (T) and extended conformation (E) are represented in teal and yellow respectively; isolated bridges are in dark yellow; degrees of helix are in pink (α-helix), blue (3-10 helix) and red (π-helix); random coils are in white.</p
<p>A) Secondary structure of helix X (residues 461–472) during simulations L1 and L2. B) Simulation ...
<p>Summary of structure prediction details of PfP2 using six different programs. Cylinders show α-he...
<p>Secondary structure of the ATP lid from the different systems was analyzed. The secondary structu...
<p>Illustrated are the WT form (A, C) and the P163S mutated form (B, D) either associated with αIIb ...
Time evolution of secondary structural elements during the MD simulations of wild-type BDNF (A) and ...
<p>(a) Time profile of secondary structural contents and (b) average (last 125 ns) secondary structu...
<p>Secondary structures are indicated by different colours in the figure: green (coil), blue (helix)...
<p><b> and </b><b>.</b> Cartoon representation of sample conformations of (a) and (b) . Purple, blu...
<p>Analysis from k2d2 program of pVHL and dVHL suggest similar secondary structure content of α-heli...
<p>The plots show the secondary structures of four peptides (axis y) in each system as a function of...
<p>Secondary structure assignments for the STAT5 proteins were averaged over the two replicas of MD ...
(A) Secondary structure breakdown of the receptor residues vs time for the last 20 ns of trajectory ...
<p>*Where: β-sheet = β-strand + β-bridge and Turn = turns + Coil. There is zero percent helix (α...
<p>(A) Aβ<sub>16−21</sub>P, (B) Aβ<sub>16−21</sub>AP (C) Aβ<sub>27−32</sub>, (D) Aβ<sub>35−42</sub> ...
Each column represents one amino acid. Extended β-strands are colored yellow, α-helices are brown, t...
<p>A) Secondary structure of helix X (residues 461–472) during simulations L1 and L2. B) Simulation ...
<p>Summary of structure prediction details of PfP2 using six different programs. Cylinders show α-he...
<p>Secondary structure of the ATP lid from the different systems was analyzed. The secondary structu...
<p>Illustrated are the WT form (A, C) and the P163S mutated form (B, D) either associated with αIIb ...
Time evolution of secondary structural elements during the MD simulations of wild-type BDNF (A) and ...
<p>(a) Time profile of secondary structural contents and (b) average (last 125 ns) secondary structu...
<p>Secondary structures are indicated by different colours in the figure: green (coil), blue (helix)...
<p><b> and </b><b>.</b> Cartoon representation of sample conformations of (a) and (b) . Purple, blu...
<p>Analysis from k2d2 program of pVHL and dVHL suggest similar secondary structure content of α-heli...
<p>The plots show the secondary structures of four peptides (axis y) in each system as a function of...
<p>Secondary structure assignments for the STAT5 proteins were averaged over the two replicas of MD ...
(A) Secondary structure breakdown of the receptor residues vs time for the last 20 ns of trajectory ...
<p>*Where: β-sheet = β-strand + β-bridge and Turn = turns + Coil. There is zero percent helix (α...
<p>(A) Aβ<sub>16−21</sub>P, (B) Aβ<sub>16−21</sub>AP (C) Aβ<sub>27−32</sub>, (D) Aβ<sub>35−42</sub> ...
Each column represents one amino acid. Extended β-strands are colored yellow, α-helices are brown, t...
<p>A) Secondary structure of helix X (residues 461–472) during simulations L1 and L2. B) Simulation ...
<p>Summary of structure prediction details of PfP2 using six different programs. Cylinders show α-he...
<p>Secondary structure of the ATP lid from the different systems was analyzed. The secondary structu...