Superposition of the rainbow-colored structure of St I (A) [5] and St II (B) [4], with the black-colored structure of StI12-31 and StII11-30 obtained by the PEP-FOLD program, respectively. Each toxin is shown at two orientations. Peptide and toxin sequence alignment and bars of RMSD values (between 0 and 1 Å) of the superimposed structures. RMSD > 1 not shown.</p
<p>Alignment was performed with MUSCLE, Signal peptide is highlighted in yellow, propeptide is highl...
<p>(A), (B) and (C): superposition of LCMV (pink) with PV (blue) structures, with the peptide in sti...
To investigate the role of the N-terminal region in the lytic mechanism of the pore-forming toxin st...
StI12-31 (A) and StII11-30 (B) structures. Colors of residues types: Non-polar (black), polar unchar...
<p>(A) <i>Left Panel</i> - Surface rendering of the SLT-1 A<sub>1</sub> chain (PDB# 1DM0) depicting ...
<p>Peptide structures were calculated in PEP-FOLD and then visualized and analyzed in Chimera softwa...
<p>Cysteine residues are shaded in black. The signal peptides and propeptides are shown in boxes. Th...
<p>Alignment of <i>Scytodes</i> venom peptides illustrating the signal sequence, propeptide, and mat...
<p>Antimicrobial peptides can be grouped into four major classes based on their secondary structures...
<p>The structural variability at each residue position for bound nonameric peptides in p-HLA complex...
<p>Core residues of each series of overlapping peptides recognized by the antivenom are colored acco...
Rational design of peptides is a challenge, which would benefit from a better knowledge of th...
<p>a. The structural alignment of minimum energy structure of the peptide bound GQYYFV-HtrA2 complex...
<p>This sequence alignment for S64 and S67 illustrates the signal sequence, linker, and mature toxin...
Solid grey bars give the RMSF for four peptides – excluding R18 – and the hatched bars give the RMSF...
<p>Alignment was performed with MUSCLE, Signal peptide is highlighted in yellow, propeptide is highl...
<p>(A), (B) and (C): superposition of LCMV (pink) with PV (blue) structures, with the peptide in sti...
To investigate the role of the N-terminal region in the lytic mechanism of the pore-forming toxin st...
StI12-31 (A) and StII11-30 (B) structures. Colors of residues types: Non-polar (black), polar unchar...
<p>(A) <i>Left Panel</i> - Surface rendering of the SLT-1 A<sub>1</sub> chain (PDB# 1DM0) depicting ...
<p>Peptide structures were calculated in PEP-FOLD and then visualized and analyzed in Chimera softwa...
<p>Cysteine residues are shaded in black. The signal peptides and propeptides are shown in boxes. Th...
<p>Alignment of <i>Scytodes</i> venom peptides illustrating the signal sequence, propeptide, and mat...
<p>Antimicrobial peptides can be grouped into four major classes based on their secondary structures...
<p>The structural variability at each residue position for bound nonameric peptides in p-HLA complex...
<p>Core residues of each series of overlapping peptides recognized by the antivenom are colored acco...
Rational design of peptides is a challenge, which would benefit from a better knowledge of th...
<p>a. The structural alignment of minimum energy structure of the peptide bound GQYYFV-HtrA2 complex...
<p>This sequence alignment for S64 and S67 illustrates the signal sequence, linker, and mature toxin...
Solid grey bars give the RMSF for four peptides – excluding R18 – and the hatched bars give the RMSF...
<p>Alignment was performed with MUSCLE, Signal peptide is highlighted in yellow, propeptide is highl...
<p>(A), (B) and (C): superposition of LCMV (pink) with PV (blue) structures, with the peptide in sti...
To investigate the role of the N-terminal region in the lytic mechanism of the pore-forming toxin st...